1ek0: Difference between revisions
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'''GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION''' | '''GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION''' | ||
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[[Category: Esters, H.]] | [[Category: Esters, H.]] | ||
[[Category: Scheidig, A J.]] | [[Category: Scheidig, A J.]] | ||
[[Category: | [[Category: Endocytosis]] | ||
[[Category: | [[Category: G protein]] | ||
[[Category: | [[Category: Gtp hydrolysis]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Vesicular traffic]] | ||
[[Category: | [[Category: Ypt/rab protein]] | ||
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Revision as of 15:11, 2 May 2008
GPPNHP-BOUND YPT51 AT 1.48 A RESOLUTION
OverviewOverview
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 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 Page seeded by OCA on Fri May 2 15:11:51 2008