1ek0: Difference between revisions

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{{STRUCTURE_1ek0|  PDB=1ek0  |  SCENE=  }}  
{{STRUCTURE_1ek0|  PDB=1ek0  |  SCENE=  }}  


'''GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION'''
===GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Vesicular traffic]]
[[Category: Vesicular traffic]]
[[Category: Ypt/rab protein]]
[[Category: Ypt/rab protein]]
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Revision as of 00:52, 1 July 2008

File:1ek0.png

Template:STRUCTURE 1ek0

GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTIONGPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION

Template:ABSTRACT PUBMED 10756108

About this StructureAbout this Structure

1EK0 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

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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