2pft
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
<StructureSection load='2pft' size='340' side='right'caption='[[2pft]], [[Resolution|resolution]] 2.25Å' scene=''> | <StructureSection load='2pft' size='340' side='right'caption='[[2pft]], [[Resolution|resolution]] 2.25Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2pft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[2pft]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PFT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2PFT FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25Å</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=2pft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pft OCA], [https://pdbe.org/2pft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pft RCSB], [https://www.ebi.ac.uk/pdbsum/2pft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pft 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=2pft FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2pft OCA], [https://pdbe.org/2pft PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2pft RCSB], [https://www.ebi.ac.uk/pdbsum/2pft PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2pft ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/EXOC7_MOUSE EXOC7_MOUSE] Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane. In adipocytes, plays a crucial role in targeting SLC2A4 vesicle to the plasma membrane in response to insulin, perhaps directing the vesicle to the precise site of fusion. It is required for neuron survival and plays an essential role in cortical development (By similarity).[UniProtKB:E7FC72]<ref>PMID:12687004</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 17: | Line 19: | ||
</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=2pft 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=2pft ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2pft" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
| Line 31: | Line 24: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Mus musculus]] |
| - | [[Category: Moore | + | [[Category: Moore BA]] |
| - | [[Category: Xu | + | [[Category: Xu Z]] |
| - | + | ||
| - | + | ||
Current revision
The Crystal Structure of Mouse Exo70 Reveals Unique Features of the Mammalian Exocyst
| |||||||||||
