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Structure paper

TitleTBC-domain GAPs for Rab GTPases accelerate GTP hydrolysis by a dual-finger mechanism.
Journal, issue, pagesNature, Vol. 442, Page 303-306, Year 2006
Publish dateFeb 27, 2006 (structure data deposition date)
AuthorsPan, X. / Eathiraj, S. / Munson, M. / Lambright, D.G.
External linksNature / PubMed:16855591
MethodsX-ray diffraction
Resolution2.26 Å
Structure data

PDB-2g77:
Crystal Structure of Gyp1 TBC domain in complex with Rab33 GTPase bound to GDP and AlF3
Method: X-RAY DIFFRACTION / Resolution: 2.26 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM

ChemComp-AF3:
ALUMINUM FLUORIDE

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • mus musculus (house mouse)
KeywordsHYDROLASE ACTIVATOR/PROTEIN TRANSPORT / Protein transport / Gyp1 TBC domain / Rab33 / vesicular trafficking / HYDROLASE ACTIVATOR-PROTEIN TRANSPORT COMPLEX

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