2d2s: Difference between revisions

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 <StructureSection load='2d2s' size='340' side='right'caption='[[2d2s]], [[Resolution|resolution]] 2.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2d2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2S FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2d2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D2S FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2b1e|2b1e]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.85&#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=2d2s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d2s OCA], [https://pdbe.org/2d2s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d2s RCSB], [https://www.ebi.ac.uk/pdbsum/2d2s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d2s ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/EXO84_YEAST EXO84_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 both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis and to the budding site. Also involved in assembly of the spliceosome.<ref>PMID:10438536</ref> <ref>PMID:11425851</ref> <ref>PMID:15788396</ref>
+[https://www.uniprot.org/uniprot/EXO84_YEAST EXO84_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 both the assembly of the exocyst and the polarization of this complex to specific sites of the plasma membrane for exocytosis and to the budding site. Also involved in assembly of the spliceosome.<ref>PMID:10438536</ref> <ref>PMID:11425851</ref> <ref>PMID:15788396</ref>
 == Evolutionary Conservation ==
 [[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=2d2s ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The exocyst is a large complex that is required for tethering vesicles at the final stages of the exocytic pathway in all eukaryotes. Here we present the structures of the Exo70p subunit of this complex and of the C-terminal domains of Exo84p, at 2.0-A and 2.85-A resolution, respectively. Exo70p forms a 160-A-long rod with a novel fold composed of contiguous alpha-helical bundles. The Exo84p C terminus also forms a long rod (80 A), which unexpectedly has the same fold as the Exo70p N terminus. Our structural results and our experimental observations concerning the interaction between Exo70p and other exocyst subunits or Rho3p GTPase are consistent with an architecture wherein exocyst subunits are composed of mostly helical modules strung together into long rods.
-The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif.,Dong G, Hutagalung AH, Fu C, Novick P, Reinisch KM Nat Struct Mol Biol. 2005 Dec;12(12):1094-100. Epub 2005 Oct 26. PMID:16249794<ref>PMID:16249794</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2d2s" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Dong, G]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Fu, C]]
+[[Category: Dong G]]
-[[Category: Hutagalung, A H]]
+[[Category: Fu C]]
-[[Category: Novick, P]]
+[[Category: Hutagalung AH]]
-[[Category: Reinisch, K M]]
+[[Category: Novick P]]
-[[Category: Endocytosis-exocytosis complex]]
+[[Category: Reinisch KM]]
-[[Category: Exo84p]]
-[[Category: Exocyst]]
-[[Category: Tethering complex]]