1ky2

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.