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spinqualitylabelsall models 1ek0, resolution 1.48Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION

Overview

Ypt/Rab proteins are membrane-associated small GTP-binding proteins which, play a central role in the coordination, activation and regulation of, vesicle-mediated transport in eukaryotic cells. We present the 1.5 A, high-resolution crystal structure of Ypt51 in its active, GppNHp-bound, conformation. Ypt51 is an important regulator involved in the endocytic, membrane traffic of Saccharomyces cerevisiae. The structure reveals small, but significant structural differences compared with H-Ras p21. The, effector loop and the catalytic loop are well defined and stabilized by, extensive hydrophobic interactions. The switch I and switch II regions, form a well-defined epitope for hypothetical effector protein binding., Sequence comparisons between the different isoforms Ypt51, Ypt52 and Ypt53, provide the first insights into determinants for specific effector binding, and for fine-tuning of the intrinsic GTP-hydrolysis rate.

About this Structure

1EK0 is a Single protein structure of sequence from Saccharomyces cerevisiae with MG, NI, GNP and GDP as ligands. Full crystallographic information is available from OCA.

Reference

High-resolution crystal structure of S. cerevisiae Ypt51(DeltaC15)-GppNHp, a small GTP-binding protein involved in regulation of endocytosis., Esters H, Alexandrov K, Constantinescu AT, Goody RS, Scheidig AJ, J Mol Biol. 2000 Apr 21;298(1):111-21. PMID:10756108

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