View source for 7jtz


==Yeast Glo3 GAP domain==
<StructureSection load='7jtz' size='340' side='right'caption='[[7jtz]], [[Resolution|resolution]] 2.07&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7jtz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7JTZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7JTZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.07&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=7jtz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7jtz OCA], [https://pdbe.org/7jtz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7jtz RCSB], [https://www.ebi.ac.uk/pdbsum/7jtz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7jtz ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GLO3_YEAST GLO3_YEAST] GTPase-activating protein for the ADP ribosylation factor (ARF) family. Involved in retrograde vesicular transport from the Golgi to the endoplasmic reticulum.<ref>PMID:9927415</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Arf GTPase activating (ArfGAP) proteins are critical regulatory and effector proteins in membrane trafficking pathways. Budding yeast contain two ArfGAP proteins (Gcs1 and Glo3) implicated in COPI coat function at the Golgi, and yeast require Glo3 catalytic function for viability. A new X-ray crystal structure of the Glo3 GAP domain was determined at 2.1 A resolution using molecular replacement methods. The structure reveals a Cys4-family zinc finger motif with an invariant residue (R59) positioned to act as an "arginine finger" during catalysis. Comparisons among eukaryotic GAP domains show a key difference between ArfGAP1 and ArfGAP2/3 family members in the final helix located within the domain. Conservation at both the sequence and structural levels suggest the Glo3 GAP domain interacts with yeast Arf1 switch I and II regions to promote catalysis. Together, the structural data presented here provide additional evidence for placing Glo3 near Arf1 triads within membrane-assembled COPI coats and further support the molecular niche model for COPI coat regulation by ArfGAPs.

The Glo3 GAP crystal structure supports the molecular niche model for ArfGAPs in COPI coats.,Xie B, Jung C, Chandra M, Engel A, Kendall AK, Jackson LP Adv Biol Regul. 2021 Jan;79:100781. doi: 10.1016/j.jbior.2020.100781. Epub 2021, Jan 5. PMID:33436318<ref>PMID:33436318</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7jtz" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae S288C]]
[[Category: Jackson LP]]
[[Category: Xie B]]