1ky3
GDP-BOUND YPT7P AT 1.35 A RESOLUTION
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OverviewOverview
The GTPase Ypt7p from S. cerevisiae is involved in late, endosome-to-vacuole transport and homotypic vacuole fusion. We present, crystal structures of the GDP- and GppNHp-bound conformation of Ypt7p, solved at 1.35 and 1.6 A resolution, respectively. Despite the similarity, of the overall structure to other Ypt/Rab proteins, Ypt7p displays small, but significant differences. The Ypt7p-specific residues Tyr33 and Tyr37, cause a difference in the main chain trace of the RabSF2 region and form a, characteristic surface epitope. Ypt7p*GppNHp does not display the helix, alpha2, characteristic of the Ras-superfamily, but instead possess an, extended loop L4/L5. Due to insertions in loops L3 and L7, the neighboring, RabSF1 and RabSF4 regions are different in their conformations to those of, other Ypt/Rab proteins.
About this StructureAbout this Structure
1KY3 is a Single protein structure of sequence from Saccharomyces cerevisiae with MG and GDP as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Rab-subfamily-specific regions of Ypt7p are structurally different from other RabGTPases., Constantinescu AT, Rak A, Alexandrov K, Esters H, Goody RS, Scheidig AJ, Structure. 2002 Apr;10(4):569-79. PMID:11937061
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