2pfv

<StructureSection load='2pfv' size='340' side='right' caption='[[2pfv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>

<table><tr><td colspan='2'>[[2pfv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2PFV FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2b1e|2b1e]], [[2b7m|2b7m]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">EXO70 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2pfv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pfv OCA], [http://pdbe.org/2pfv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2pfv RCSB], [http://www.ebi.ac.uk/pdbsum/2pfv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2pfv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/EXO70_YEAST EXO70_YEAST]] Involved in the secretory pathway as part of the exocyst complex which tethers secretory vesicles to the sites of exocytosis. Plays a role in the assembly of the exocyst.<ref>PMID:15583030</ref>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/pf/2pfv_consurf.spt"</scriptWhenChecked>

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== Publication Abstract from PubMed ==

The exocyst is a eukaryotic tethering complex necessary for the fusion of exocytic vesicles with the plasma membrane. Its function in vivo is tightly regulated by interactions with multiple small GTPases. Exo70, one of the eight subunits of the exocyst, is important for the localization of the exocyst to the plasma membrane. It interacts with TC10 and Rho3 GTPases in mammals and yeast, respectively, and has been shown recently to bind to the actin-polymerization complex Arp2/3. Here, we present the crystal structure of Mus musculus Exo70 at 2.25 A resolution. Exo70 is composed of alpha-helices in a series of right-handed helix-turn-helix motifs organized into a long rod of length 170 A and width 35 A. Although the alpha-helical organization of this molecule is similar to that in Saccharomyces cerevisiae Exo70, major structural differences are observed on the surface of the molecule, at the domain boundaries, and in various loop structures. In particular, the C-terminal domain of M. musculus Exo70 adopts a new orientation relative to the N-terminal half not seen in S. cerevisiae Exo70 structures. Given the low level of sequence conservation within Exo70, this structure provides new insights into our understanding of many species-specific functions of the exocyst.

The crystal structure of mouse Exo70 reveals unique features of the mammalian exocyst.,Moore BA, Robinson HH, Xu Z J Mol Biol. 2007 Aug 10;371(2):410-21. Epub 2007 May 22. PMID:17583731<ref>PMID:17583731</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 2pfv" style="background-color:#fffaf0;"></div>

[[Category: Atcc 18824]]

[[Category: Moore, B A]]

[[Category: Robinson, H H]]

[[Category: Xu, Z]]

[[Category: Endocytosis-exocytosis complex]]

[[Category: Helix-turn-helix]]