2b1e: Difference between revisions
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<StructureSection load='2b1e' size='340' side='right'caption='[[2b1e]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='2b1e' size='340' side='right'caption='[[2b1e]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2b1e]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2b1e]] 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=2B1E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B1E FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d2s|2d2s]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2d2s|2d2s]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b1e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b1e OCA], [https://pdbe.org/2b1e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b1e RCSB], [https://www.ebi.ac.uk/pdbsum/2b1e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b1e ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://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> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 16:04, 24 November 2021
The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motifThe structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif
Structural highlights
Function[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.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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