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Information on EC 2.7.1.164 - O-phosphoseryl-tRNASec kinase
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2.7.1.164 O-phosphoseryl-tRNASec kinaseIUBMB Comments
In archaea and eukarya selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by EC 2.9.1.2 (Sep-tRNA:Sec-tRNA synthase).
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Word Map
- 2.7.1.164
- selenocysteine
-
selenoproteins
-
sep-trna:sec-trna
- selenophosphate
- jannaschii
- sepsecs
-
decoding
-
serylates
-
ser-trnasec
-
methanocaldococcus
-
methanococcus
-
anticodon
-
aminoacylated
-
trna-dependent
- selenide
-
selenocysteine-specific
-
selenocysteinyl-trna
- eukarya
-
trnasersec
- aminoacyl-trnas
- maripaludis
-
d-stem
-
aa-trnas
-
amidotransferases
- amppnp
- trnaser
-
misacylated
- serrs
The expected taxonomic range for this enzyme is: Archaea, Eukaryota
Synonyms
o-phosphoseryl-trna(sec) kinase, o-phosphoseryl-trna kinase, phosphoseryl-trna[ser]sec kinase, phosphoseryl-trnasec kinase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
O-phosphoseryl-tRNA kinase
O-phosphoseryl-tRNA(Sec) kinase
O-phosphoseryl-tRNASec kinase
phosphoseryl-tRNASec kinase
PSTK
Tb10.6k15.1110
TbPSTK
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + L-seryl-tRNASec = ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-seryl-tRNASec O-phosphotransferase
In archaea and eukarya selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous L-seryl-tRNASec to O-phospho-L-seryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by EC 2.9.1.2 (Sep-tRNA:Sec-tRNA synthase).
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CAS REGISTRY NUMBER
COMMENTARY
91273-83-5
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
GTP + L-seryl-tRNASec
GDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 40% the activity of ATP
-
-
?
ITP + L-seryl-tRNASec
IDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 85% the activity of ATP
-
-
?
UTP + L-seryl-tRNASec
UDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 40% the activity of ATP
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
the enzyme does not recognize free Ser as a substrate for phosphate transfer. Ser attached to tRNASec is its obligate substrate. Neither tRNASer nor L-seryl-tRNASer is a substrate for phosphorylation
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
the enzyme does not recognize free Ser as a substrate for phosphate transfer. Ser attached to tRNASec is its obligate substrate. Neither tRNASer nor L-seryl-tRNASer is a substrate for phosphorylation
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
Pstk is a limiting factor for hepatic selenoprotein biosynthesis, and its mRNA expression is most strongly affected during the lipopolysaccharide (LPS)-induced acute-phase response
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
about 30% of O-phospho-L-seryltRNA[Ser]Sec is converted to L-seryl-tRNA[Ser]Sec and ATP during the course of the reaction. The kinase is specific for the two major isoforms of O-phospho-L-seryl-tRNA[Ser]Sec. Seryl-tRNA1Ser does not serve as a substrate for PSTK
-
-
r
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
null mutants of PSTK abolish selenoprotein synthesis, demonstrating the essentiality of the enzyme for the formation of L-selenocysteinyl-tRNASec. Growth of the knockout strain is not impaired. Thus, unlike mammals, trypanosomes do not require selenoproteins for viability
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
O-phospho-L-seryl-tRNASec + ADP
PSTK distinguishes tRNASec from tRNASer. Unlike eukaryotic PSTK, the archaeal enzyme recognizes the acceptor stem rather than the length and secondary structure of the D-stem. The seryl moiety of L-seryl-tRNASec is not required for enzyme recognition, as PSTK efficiently phosphorylates L-threonyl-tRNASec
-
-
?
ATP + L-seryl-tRNASec
O-phospho-L-seryl-tRNASec + ADP
PSTK distinguishes tRNASec from tRNASer. Unlike eukaryotic PSTK, the archaeal enzyme recognizes the acceptor stem rather than the length and secondary structure of the D-stem. The seryl moiety of L-seryl-tRNASec is not required for enzyme recognition, as PSTK efficiently phosphorylates L-threonyl-tRNASec
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
CTP + L-seryl-tRNASec
CDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 60% the activity of ATP
-
-
?
CTP + L-seryl-tRNASec
CDP + O-phospho-L-seryl-tRNASec
phosphorylation at about 60% the activity of ATP
-
-
?
dATP + L-seryl-tRNASec
dADP + O-phospho-L-seryl-tRNASec
phosphorylation at about 65% the activity of ATP
-
-
?
dATP + L-seryl-tRNASec
dADP + O-phospho-L-seryl-tRNASec
phosphorylation at about 65% the activity of ATP
-
-
?
L-threonyl-tRNASec + ATP
O-phospho-L-threonyl-tRNASec + ADP
-
-
-
?
L-threonyl-tRNASec + ATP
O-phospho-L-threonyl-tRNASec + ADP
-
-
-
?
additional information
?
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
additional information
?
-
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
additional information
?
-
no phosphorylation activity with 5'-adenylyl (beta,gamma-methylene)diphosphonate, very low phosphorylation activity with alpha,beta-methyleneadenosine 5'-triphosphate
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
Pstk is a limiting factor for hepatic selenoprotein biosynthesis, and its mRNA expression is most strongly affected during the lipopolysaccharide (LPS)-induced acute-phase response
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
null mutants of PSTK abolish selenoprotein synthesis, demonstrating the essentiality of the enzyme for the formation of L-selenocysteinyl-tRNASec. Growth of the knockout strain is not impaired. Thus, unlike mammals, trypanosomes do not require selenoproteins for viability
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + L-seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
-
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
ATP + seryl-tRNASec
ADP + O-phospho-L-seryl-tRNASec
L-phosphoseryl-tRNA is the crucial precursor for L-selenocysteinyl-tRNA formation in archaea and eukarya. Selenocysteine formation is achieved by a two-step process: O-phosphoseryl-tRNASec kinase (PSTK) phosphorylates the endogenous Ser-tRNASec to O-phosphoseryl-tRNASec, and then this misacylated amino acid-tRNA species is converted to L-selenocysteinyl-tRNASec by Sep-tRNA:Sec-tRNA synthase (SepSecS)
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mn2+ can replace Mg2+ as a divalent metal cation, but it is not as efficient as Mg2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
additional information
subcellular localization and complex formation analysis of enzyme PSTK, overview
-
brenda
additional information
-
subcellular localization and complex formation analysis of enzyme PSTK, overview
-
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
malfunction
-
knockdown of TbPSTK impairs selenoprotein synthesis in the parasite procyclic form (PCF). TbPSTK and TbSEPSECS double-knockout cell lines demonstrate that Trypanosoma brucei parasite procyclic form does not depend on selenoproteins
-
metabolism
the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
metabolism
-
the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
metabolism
selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
metabolism
-
the enzyme is involved in the selenocysteine incorporation pathway in this primitive eukaryote
-
metabolism
-
the synthesis of selenocysteine, the 21st amino acid, occurs on its transfer RNA, tRNASec. tRNASec is initially aminoacylated with serine by seryl-tRNA synthetase and the resulting seryl moiety is converted to phosphoserine by O-phosphoseryl-tRNA kinase (PSTK) in eukaryotes. The selenium donor, selenophosphate is synthesized from selenide and ATP by selenophosphate synthetase. Selenocysteinyl-tRNA synthase (Sep-SecS) then uses the O-phosphoseryl-tRNASec and selenophosphate to form Sec-tRNASec in eukaryotes. Leishmania SepSecS enzyme is active and able to complement the DELTAselA deletion in Escherichia coli JS1 strain only in the presence of archaeal PSTK, indicating the conserved nature of the PSTK-SepSecS pathway, selenocysteinyl-tRNA synthase is dependent on the action of PSTK enzyme in the Sec insertion pathway
-
metabolism
-
selenocysteine biosynthesis and incorporation into selenoproteins require an intricate molecular machinery that is present, but not ubiquitous, in all domains of life. In eukaryotes it begins with tRNA[Ser]Sec acylation with L-serine by the seryl-tRNA synthetase (SerRS) followed by its conversion to Sec-tRNA[Ser]Sec, sequentially catalyzed by phosphoseryl-tRNASec kinase (PSTK) and Sec-tRNA[Ser]Sec synthase (SEPSECS). Selenophosphate synthetase (SEPHS) is a key enzyme in the Sec pathway, being responsible for catalyzing the formation of the active selenium donor for this reaction, selenophosphate, from selenide and ATP. Enzyme phosphoseryl-tRNASec kinase (PSTK) forms a stable complex with the Sec-tRNASec synthase (SEPSECS)
-
physiological function
the enzyme is involved in the biosynthesis of selenocysteine
physiological function
-
the enzyme is essential in the selenocysteine insertion
physiological function
-
the enzyme is involved in the biosynthesis of selenocysteine
-
physiological function
-
the enzyme is essential in the selenocysteine insertion
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PSTK_HUMAN
348
0
39527
Swiss-Prot
other Location (Reliability: 3)
PSTK_METJA
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
248
0
29467
Swiss-Prot
-
PSTK_METKA
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
255
0
29790
Swiss-Prot
-
PSTK_METMP
Methanococcus maripaludis (strain S2 / LL)
255
0
29776
Swiss-Prot
-
PSTK_MOUSE
359
0
40763
Swiss-Prot
Mitochondrion (Reliability: 5)
A0A8B6EWS6_MYTGA
344
0
39024
TrEMBL
other Location (Reliability: 2)
I2CRI4_NANGC
Nannochloropsis gaditana (strain CCMP526)
338
0
38401
TrEMBL
Secretory Pathway (Reliability: 5)
A0A113QNR3_PLABE
540
0
65699
TrEMBL
other Location (Reliability: 3)
B2GUE1_XENTR
374
0
42183
TrEMBL
Mitochondrion (Reliability: 3)
A0A1Q9NL27_THOAA
Thorarchaeota archaeon (strain AB_25)
249
0
28793
TrEMBL
-
A0A150J3M2_9EURY
164
0
18971
TrEMBL
-
A0A6J8F0S9_MYTCO
311
0
35192
TrEMBL
other Location (Reliability: 3)
A0A1G4GRF0_PLAVI
575
0
67554
TrEMBL
other Location (Reliability: 3)
A0A150JG54_9EURY
164
0
19050
TrEMBL
-
A0A812CY58_SEPPH
290
0
33354
TrEMBL
other Location (Reliability: 1)
Q8I2A3_PLAF7
535
0
65607
TrEMBL
other Location (Reliability: 3)
A0A060RMT0_PLARE
541
0
66466
TrEMBL
other Location (Reliability: 3)
A0A653HND1_9APIC
538
0
65667
TrEMBL
other Location (Reliability: 3)
A0A6J8F3N9_MYTCO
328
0
37593
TrEMBL
other Location (Reliability: 3)
A0A7R8D6V8_LEPSM
142
0
16076
TrEMBL
other Location (Reliability: 2)
A0A1D3LAU9_PLACH
540
0
64397
TrEMBL
other Location (Reliability: 4)
A0A5B9DD47_9ARCH
295
0
34495
TrEMBL
-
A0A833E461_9EURY
257
0
31085
TrEMBL
-
A0A832ZYL8_9EURY
251
0
29910
TrEMBL
-
A0A1A7W2Z0_PLAKH
535
0
64116
TrEMBL
other Location (Reliability: 2)
A0A1J1GLT9_PLAGA
507
0
63071
TrEMBL
other Location (Reliability: 3)
A0A1V6INE5_9EURY
164
0
19050
TrEMBL
-
A0A6J8F3T5_MYTCO
344
0
39386
TrEMBL
other Location (Reliability: 3)
A0A679KT63_PLAKH
535
0
64116
TrEMBL
other Location (Reliability: 2)
A0A1Z5JEZ8_FISSO
336
0
38662
TrEMBL
other Location (Reliability: 2)
A0A150J0A4_9EURY
164
0
18795
TrEMBL
-
A0A1C6X1V3_PLACH
540
0
64381
TrEMBL
other Location (Reliability: 4)
A0A078K5T6_PLAYE
572
0
68354
TrEMBL
other Location (Reliability: 4)
A0A1G4H6Y2_PLAVI
575
0
67524
TrEMBL
other Location (Reliability: 3)
A0A1D3LEB4_PLACH
540
0
64498
TrEMBL
other Location (Reliability: 4)
A0A061ICD5_CRIGR
358
0
40702
TrEMBL
other Location (Reliability: 4)
A0A061IEX8_CRIGR
346
0
39127
TrEMBL
other Location (Reliability: 4)
A0A8B6EY34_MYTGA
352
0
39753
TrEMBL
other Location (Reliability: 2)
A0A150IWP6_9EURY
164
0
19011
TrEMBL
-
A0A832Z7D6_9EURY
257
0
31051
TrEMBL
-
A0A1Z5KNE8_FISSO
336
0
38716
TrEMBL
other Location (Reliability: 1)
A0A1C6X7T0_PLACH
540
0
64469
TrEMBL
other Location (Reliability: 4)
Q38A45_TRYB2
Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
360
0
40101
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with an anticodon-stem/loop truncated tRNASec, to 2.4 A resolution. Truncated tRNASec is bound between the enzyme's C-terminal domain CTD and N-terminal kinase domain NTD that are connected by a flexible 11 amino acid linker. Upon tRNASec recognition, the CTD undergoes a 62-A movement to allow proper binding of the 7-bp D-stem. This large reorganization of the quaternary structure likely provides a means by which the unique tRNASec species can be accurately recognized with high affinity by the translation machinery
in complex with Methanopyrus tRNASec and with 5'-adenylyl imidodiphosphate, to 2.5-2.9 A resolution. The enzyme consists of two independent linker-connected domains, the N-terminal catalytic domain NTD and the C-terminal domain CTD. The D-arm-CTD binding occurs independently of and much more strongly than the acceptor-arm-NTD binding. The enzyme thereby distinguishes the characteristic D arm with the maximal stem and the minimal loop of tRNASec from the canonical D arm of tRNASer, without interacting with the anticodon
sitting drop vapor diffusion method at 20°C, the structures of MjPSTK complexed with ADP and AMPPNP revealed that this enzyme belongs to the P-loop kinase class, and that the kinase domain is closely related to gluconate kinase and adenylate kinase. ATP is bound by the P-loop domain (residues 11-18). Formed by antiparallel dimerization of two O-phosphoseryl-tRNASec kinase monomers, the enzyme structure shows a deep groove with positive electrostatic potential. Located in this groove is the active site of the enzyme, which biochemical and genetic data suggest is composed of Asp-41, Arg-44, Glu-55, Tyr-82, Tyr-83, Met-86, and Met-132
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K142A/Y143A
mutant shows severely reduced activity with the Methanopyrus kandleri tRNASec substrate
K17A
R116A
mutant enzyme is 23.5fold less active than wild-type enzyme
S18A
T19W
mutant enzyme is 2.8fold less active than wild-type enzyme
R116A
-
mutant enzyme is 23.5fold less active than wild-type enzyme
-
S18A
T19W
-
mutant enzyme is 2.8fold less active than wild-type enzyme
-
additional information
K17A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
mutation abolishes catalytic activity and and inhibits tRNASec recognition
S18A
-
mutation abolishes catalytic activity and and inhibits tRNASec recognition
-
additional information
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
-
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
additional information
-
truncation of the C-termional domain. Deletions of up to 98 amino acids, PSTK1-153, still show activity, albeit at a much reduced level of about 6% of the initial velocity of the intact enzyme. In vivo, PSTK1-153 is still able compensate for the Escherichia coli selA deletion. Truncation PSTK1-192 lacks the entire CTD domain and exhibits 40% residual activity. PSTK1-215 and PSTK1-240 mutants lack the terminal two and one helices of the helix bundle, respectively. PSTK1-215 mutant shows remarkably reduced activity
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
gene PSTK, DNA and amino acid sequence determination and analysis, RT-PCR
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kaiser, J.T.; Gromadski, K.; Rother, M.; Engelhardt, H.; Rodnina, M.V.; Wahl, M.C.
Structural and functional investigation of a putative archaeal selenocysteine synthase
Biochemistry
44
13315-13327
2005
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Renko, K.; Hofmann, P.J.; Stoedter, M.; Hollenbach, B.; Behrends. T.; Khrle, J.; Schweizer, U.; Schomburg, L.
Down-regulation of the hepatic selenoprotein biosynthesis machinery impairs selenium metabolism during the acute phase response in mice
FASEB J.
23
1758-1765
2009
Mus musculus (Q8BP74)
brenda
Sherrer, R.L.; O'Donoghue, P.; Sll D.
Characterization and evolutionary history of an archaeal kinase involved in selenocysteinyl-tRNA formation
Nucleic Acids Res.
36
1247-1259
2008
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Sherrer, R.L.; Ho, J.M.; Sll, D.
Divergence of selenocysteine tRNA recognition by archaeal and eukaryotic O-phosphoseryl-tRNASec kinase
Nucleic Acids Res.
36
1871-1880
2008
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Carlson, B.A.; Xu, X.M.; Kryukov, G.V.; Rao, M.; Berry, M.J.; Gladyshev, V.N.; Hatfield, D.L.
Identification and characterization of posphoseryl-tRNA[Ser]Sec kinase
Proc. Natl. Acad. Sci. USA
101
12848-12853
2004
Mus musculus (Q8BP74), Mus musculus
brenda
Yuan, J.; Palioura, S.; Salazar, J.C.; Su, D.; O'Donoghue, P.; Hohn, M.J.; Cardoso, A.M.; Whitman, W.B.; Sll, D.
RNA-dependent conversion of phosphoserine forms selenocysteine in eukaryotes and archaea
Proc. Natl. Acad. Sci. USA
103
18923-18927
2006
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Aeby, E.; Palioura, S.; Pusnik, M.; Marazzi, J.; Lieberman, A.; Ullu, E.; Sll, D.; Schneider, A.
The canonical pathway for selenocysteine insertion is dispensable in Trypanosomes
Proc. Natl. Acad. Sci. USA
106
5088-5092
2009
Trypanosoma brucei
brenda
Chiba, S.; Itoh, Y.; Sekine, S.; Yokoyama, S.
Structural basis for the major role of O-phosphoseryl-tRNA kinase in the UGA-specific encoding of selenocysteine
Mol. Cell
39
410-420
2010
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Sherrer, R.L.; Araiso, Y.; Aldag, C.; Ishitani, R.; Ho, J.M.; Soell, D.; Nureki, O.
C-terminal domain of archaeal O-phosphoseryl-tRNA kinase displays large-scale motion to bind the 7-bp D-stem of archaeal tRNA(Sec)
Nucleic Acids Res.
39
1034-1041
2011
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Araiso, Y.; Sherrer, R.L.; Ishitani, R.; Ho, J.M.; Sll, D.; Nureki, O.
Structure of a tRNA-dependent kinase essential for selenocysteine decoding
Proc. Natl. Acad. Sci. USA
106
16215-16220
2009
Methanocaldococcus jannaschii (Q58933), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (Q58933)
brenda
Manhas, R.; Gowri, V.S.; Madhubala, R.
Leishmania donovani encodes a functional selenocysteinyl-tRNA synthase
J. Biol. Chem.
291
1203-1220
2016
Leishmania donovani
brenda
da Silva, M.T.; Caldas, V.E.; Costa, F.C.; Silvestre, D.A.; Thiemann, O.H.
Selenocysteine biosynthesis and insertion machinery in Naegleria gruberi
Mol. Biochem. Parasitol.
188
87-90
2013
Naegleria gruberi (D2V263), Naegleria gruberi ATCC 30224 (D2V263)
brenda
da Silva, M.; E. Silva, I.; Faim, L.; Bellini, N.; Pereira, M.; Lima, A.; de Jesus, T.; Costa, F.; Watanabe, T.; Pereira, H.; Valentini, S.; Zanelli, C.; Borges, J.; Dias, M.; da Cunha, J.; Mittra, B.; Andrews, N.; Thiemann, O.
Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase
PLoS Negl. Trop. Dis.
14
1-31
2020
Trypanosoma brucei brucei (Q38A45), Trypanosoma brucei brucei 927/4 GUTat10.1 (Q38A45)
brenda
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Release 2023.1 (January 2023)
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