2a2f

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2a2f, resolution 2.50Å

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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

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