View source for 7urr


==Gea2 closed/open conformation (composite structure)==
<StructureSection load='7urr' size='340' side='right'caption='[[7urr]], [[Resolution|resolution]] 4.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7urr]] is a 2 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=7URR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7URR FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.7&#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=7urr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7urr OCA], [https://pdbe.org/7urr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7urr RCSB], [https://www.ebi.ac.uk/pdbsum/7urr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7urr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GEA2_YEAST GEA2_YEAST] Activates the ARF proteins by exchanging bound GDP for free GTP.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf guanosine triphosphatases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins. Arf activation and Golgi membrane association is controlled by large guanine nucleotide exchange factors (GEFs) possessing multiple conserved regulatory domains. Here we present cryoelectron microscopy (cryoEM) structures of full-length Gea2, the yeast paralog of the human Arf-GEF GBF1, that reveal the organization of these regulatory domains and explain how Gea2 binds to the Golgi membrane surface. We find that the GEF domain adopts two different conformations compatible with different stages of the Arf activation reaction. The structure of a Gea2-Arf1 activation intermediate suggests that the movement of the GEF domain primes Arf1 for membrane insertion upon guanosine triphosphate binding. We propose that conformational switching of Gea2 during the nucleotide exchange reaction promotes membrane insertion of Arf1.

Structural basis for activation of Arf1 at the Golgi complex.,Muccini AJ, Gustafson MA, Fromme JC Cell Rep. 2022 Aug 30;40(9):111282. doi: 10.1016/j.celrep.2022.111282. PMID:36044848<ref>PMID:36044848</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7urr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Fromme JC]]
[[Category: Muccini A]]