2a2f

<StructureSection load='2a2f' size='340' side='right' caption='[[2a2f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[2a2f]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2A2F FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sec15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2f OCA], [http://pdbe.org/2a2f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2a2f RCSB], [http://www.ebi.ac.uk/pdbsum/2a2f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2f ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/EXOC6_DROME EXOC6_DROME]] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:16155582</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 2a2f" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Drome]]

[[Category: Bellen, H J]]

[[Category: Mehta, S Q]]

[[Category: Pichaud, F]]

[[Category: Quiocho, F A]]

[[Category: Wu, S]]

[[Category: All helical structure]]

[[Category: Protein transport]]