2a2f
From Proteopedia
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'''Crystal Structure of Sec15 C-terminal domain''' | '''Crystal Structure of Sec15 C-terminal domain''' | ||
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[[Category: Quiocho, F A.]] | [[Category: Quiocho, F A.]] | ||
[[Category: Wu, S.]] | [[Category: Wu, S.]] | ||
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Revision as of 15:31, 3 May 2008
Crystal Structure of Sec15 C-terminal domain
Overview
Sec15, a component of the exocyst, recognizes vesicle-associated Rab GTPases, helps target transport vesicles to the budding sites in yeast and is thought to recruit other exocyst proteins. Here we report the characterization of a 35-kDa fragment that comprises most of the C-terminal half of Drosophila melanogaster Sec15. This C-terminal domain was found to bind a subset of Rab GTPases, especially Rab11, in a GTP-dependent manner. We also provide evidence that in fly photoreceptors Sec15 colocalizes with Rab11 and that loss of Sec15 affects rhabdomere morphology. Determination of the 2.5-A crystal structure of the C-terminal domain revealed a novel fold consisting of ten alpha-helices equally distributed between two subdomains (N and C subdomains). We show that the C subdomain, mainly via a single helix, is sufficient for Rab binding.
About this Structure
2A2F is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.
Reference
Sec15 interacts with Rab11 via a novel domain and affects Rab11 localization in vivo., Wu S, Mehta SQ, Pichaud F, Bellen HJ, Quiocho FA, Nat Struct Mol Biol. 2005 Oct;12(10):879-85. Epub 2005 Sep 11. PMID:16155582 Page seeded by OCA on Sat May 3 18:31:03 2008
