2a2f

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Current revision (09:10, 14 February 2024) (edit) (undo)
 
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<StructureSection load='2a2f' size='340' side='right'caption='[[2a2f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='2a2f' size='340' side='right'caption='[[2a2f]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2a2f]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=2A2F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2a2f]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. 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 [https://proteopedia.org/fgij/fg.htm?mol=2A2F FirstGlance]. <br>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sec15 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2f OCA], [https://pdbe.org/2a2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a2f RCSB], [https://www.ebi.ac.uk/pdbsum/2a2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2f ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a2f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2f OCA], [https://pdbe.org/2a2f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a2f RCSB], [https://www.ebi.ac.uk/pdbsum/2a2f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://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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[https://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.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a2f ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2a2f ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 2a2f" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Drome]]
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[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bellen, H J]]
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[[Category: Bellen HJ]]
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[[Category: Mehta, S Q]]
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[[Category: Mehta SQ]]
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[[Category: Pichaud, F]]
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[[Category: Pichaud F]]
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[[Category: Quiocho, F A]]
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[[Category: Quiocho FA]]
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[[Category: Wu, S]]
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[[Category: Wu S]]
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[[Category: All helical structure]]
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[[Category: Protein transport]]
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Current revision

Crystal Structure of Sec15 C-terminal domain

PDB ID 2a2f

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