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Literature summary extracted from

  • Ganichkin, O.M.; Xu, X.M.; Carlson, B.A.; Mix, H.; Hatfield, D.L.; Gladyshev, V.N.; Wahl, M.C.
    Structure and catalytic mechanism of eukaryotic selenocysteine synthase (2008), J. Biol. Chem., 283, 5849-5865.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.9.1.1 expression of SecS as C-terminally His6-tagged enzyme in Escherichia coli strain Rosetta2(DE3) Mus musculus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.9.1.1 purified recombinant C-terminally His6-tagged SecS, apoenzyme or in complex with phosphate or iodide, sitting-drop vapor diffusion at 20°C, 14 mg/ml protein in 10 mM HEPES-NaOH, pH 7.5, 500 mM NaCl, 2 mM DTT, is mixed with an equal volume of reservoir solution containing 11% v/v ethylene glycol without other buffer components, 2 days, cryoprotection by crystal soaking in 100 mM HEPES-NaOH, pH 7.5, 250 mM NaCl, 1 mM dithiothreitol, and 35% v/v ethylene glycol, X-ray diffraction structure determination and analysis at 1.65-2.38 A resolution Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.9.1.1 20000
-
 about, gel filtration Mus musculus
2.9.1.1 49000
-
 4 * 49000, SDS-PAGE Mus musculus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.9.1.1 L-seryl-tRNASec + selenophosphate Mus musculus
-
 L-selenocysteinyl-tRNASec + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.9.1.1 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.9.1.1 recombinant C-terminally His6-tagged SecS from Escherichia coli strain Rosetta2(DE3) by nickel affinity chromatography and gel filtration to over 95% purity Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
2.9.1.1 L-seryl-tRNASec + selenophosphate = L-selenocysteinyl-tRNASec + phosphate substrate binding and reaction mechanism Mus musculus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.9.1.1 L-seryl-tRNASec + selenophosphate
-
 Mus musculus L-selenocysteinyl-tRNASec + phosphate
-
 ?
2.9.1.1 L-seryl-tRNASec + selenophosphate the phosphate loop accommodates the gamma-phosphate moiety of O-phospho-L-seryltRNA [Ser]Sec and, after phosphate elimination, binds selenophosphate to initiate attack on the proposed aminoacrylyltRNA [Ser]Sec intermediate. Binding of phosphate triggers disorder-order transition in an active site loop Mus musculus L-selenocysteinyl-tRNASec + phosphate
-
 ?
2.9.1.1 additional information SecS does not act on free O-phospho-L-serine Mus musculus ?
-
 ?

Subunits

EC Number Subunits Comment Organism
2.9.1.1 More two SecS monomers interact intimately and together build up two identical active sites around PLP in a Schiff-base linkage with Lys284. Two SecS dimers further associate to form a homotetramer. The N-terminus, which mediates tetramer formation, and a large insertion that remodels the active site set SecS aside from other members of the family Mus musculus
2.9.1.1 tetramer 4 * 49000, SDS-PAGE Mus musculus

Synonyms

EC Number Synonyms Comment Organism
2.9.1.1 More SecS is a member of the fold type I family of PLP-dependent enzymes with distinct structural elements Mus musculus
2.9.1.1 SecS
-
 Mus musculus
2.9.1.1 Selenocysteine synthase
-
 Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.9.1.1 pyridoxal 5'-phosphate SecS is a a PLP-dependent transferase. The PLP cofactor iIs tightly anchored by non-canonical contacts to both protomers of a close dimer Mus musculus