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- W2036408082 abstract "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 Å 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 α2, 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." @default.
- W2036408082 created "2016-06-24" @default.
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- W2036408082 date "2002-04-01" @default.
- W2036408082 modified "2023-10-14" @default.
- W2036408082 title "Rab-Subfamily-Specific Regions of Ypt7p Are Structurally Different from Other RabGTPases" @default.
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- W2036408082 doi "https://doi.org/10.1016/s0969-2126(02)00737-2" @default.
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