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Literature summary for 3.6.5.5 extracted from

  • Yan, L.; Sun, S.; Wang, W.; Shi, J.; Hu, X.; Wang, S.; Su, D.; Rao, Z.; Hu, J.; Lou, Z.
    Structures of the yeast dynamin-like GTPase Sey1p provide insight into homotypic ER fusion (2015), J. Cell Biol., 210, 961-972.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.6.5.5

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of truncated enzyme Sey1p(1-692) in Escherichia coli, recombinant expressioj of Myc-tagged scSey1p in COS-7 cells and immunolocalization study Candida albicans

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant truncated enzyme Sey1p(1-692) , wild-type or selenomethionine-labeled, in complex with GDP, GMP-PNP, or GDP plus AlF4-, X-ray diffraction structure determination and analysis at 2.3-3.0 A resolution Candida albicans

Protein Variants

Protein Variants Comment Organism
L233A site-directed mutagensis, the mutation drastically reduces the dimerization, GTPase activity, and fusion activity of scSey1p Candida albicans
additional information generation of a truncation mutant comprising residues 1-692. The mutant is truncated before the first transmembrane region Candida albicans

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum membrane membrane-anchored by two closely spaced transmembrane segments, exposing both termini to the cytosol Candida albicans 5789
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endoplasmic reticulum tubule
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 Candida albicans
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-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required for activity, especially for the membrane fusion activity Candida albicans

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + H2O Candida albicans
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 GDP + phosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Candida albicans Q9C0L9
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-

Purification (Commentary)

Purification (Comment) Organism
recombinant truncated enzyme Sey1p(1-692) from Escherichia coli Candida albicans

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + H2O
-
 Candida albicans GDP + phosphate
-
 ?
additional information the enzyme mediates homotypic membrane fusion of the endoplasmic reticulum, wild-type scSey1p shows efficient fusion in the presence of GTP and Mg2+. No fusion is seen with GDP or in the absence of Mg2+. Addition of GMP-PNP caused moderate but reproducible fusion. Nucleotide-dependent conformational changes of Sey1p, nucleotide binding structure, detailed overview Candida albicans ?
-
 ?

Subunits

Subunits Comment Organism
More enzyme Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AIF4-, but is monomeric with GDP. The dimerization of caSey1p involves a hydrophobic patch on top of the GTPase domain, including a conserved L257 within the guanine cap, and several hydrophilic interactions along the GTPase interface. The stalk domains also pack against each other in the dimer Candida albicans

Synonyms

Synonyms Comment Organism
caSey1p
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 Candida albicans
dynamin-like GTPase
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 Candida albicans
dynamin-like guanosine triphosphatase
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 Candida albicans
Sey1p
-
 Candida albicans

General Information

General Information Comment Organism
evolution the enzyme belongs to the dynamin superfamily Candida albicans
malfunction deletion of Sey1p protein in cells results in unbranched endoplasmic reticulum, delayed endoplasmic reticulum fusion, or even endoplasmic reticulum fragmentation. Deletion of Sey1p results in decreased virulence Candida albicans
metabolism enzyme Sey1p can replace the dynamin-like GTPase atlastin (ATL) in mammalian cells Candida albicans
additional information the enzyme has a long stalk-like, helical bundle domain. Structures of the cytosolic domain of Sey1p, overview. Enzyme CytSey1p consists of an N-terminal GTPase domain and a long, stalk-like, helical domain connected by a linker region. In the dimer, the GTPase domains interact with one another in such a way that the nucleotide binding sites face each other. The linker regions of the two Sey1p molecules cross one another, allowing a close association of the tops of the stalk domains. The stalk domain is composed of four three-helix bundles, with the last helix of each bundle extending into the first helix of the next bundle. The catalytic residues is S68 in caSey1p, which adopts a different rotamer conformation after the cleavage of the gamma-phosphate bond, which in turn causes some minor local rearrangements Candida albicans
physiological function the enzyme mediates homotypic membrane fusion of the endoplasmic reticulum, GTP hydrolysis is not essential but accelerates the fusion reaction, the proposed mechanism demonstrates a common scheme for fusion mediated by dynamin-like GTPases and reveals that the stalk domain of Sey1p possesses unique functional features. The linkage of opposing membranes through GTP binding-induced dimerization may be sufficient to promote Sey1p-mediated fusion. GTPase-based endoplasmic reticulum fusogens play critical physiological roles Candida albicans