4oiy
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 4oiy is ON HOLD Authors: Qiu, B., Zhang, K., Sun, F. Description: Crystal structure of Sec7p catalytic domain) |
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of Sec7p catalytic domain== | |
| + | <StructureSection load='4oiy' size='340' side='right'caption='[[4oiy]], [[Resolution|resolution]] 1.50Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4oiy]] is a 2 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=4OIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OIY 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]] 1.5Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4oiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oiy OCA], [https://pdbe.org/4oiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oiy RCSB], [https://www.ebi.ac.uk/pdbsum/4oiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oiy ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SEC7_YEAST SEC7_YEAST] May play a role in vesicular budding and traffic between compartments of the Golgi apparatus. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | ADP-ribosylation factors (Arfs) play key roles in controlling membrane traffic and organelle structures. The activation of Arfs from GDP to GTP binding form is triggered by the guanine exchange factors (GEFs). There are six families of Arf-GEFs with a common guanine exchange catalytic domain (Sec7 domain) and various mechanisms of guanine exchange activity regulation. A loop region (loop>J motif) just following the helix J of Sec7 domain was found conserved and important for the catalytic activity regulation of Arf-GEFs. However, the molecular detail of the role the loop>J motif plays has been yet unclear. Here, we studied the catalytic domain of Sec7p, a yeast trans-Golgi network membrane localized Arf-GEFs, and found that the loop>J motif is indispensible for its GEF catalytic activity. Crystallographic, NMR spectrum and mutagenesis studies suggested that the loop>J motif with a key conserved residue Ile1010 modulates the fine conformation of Sec7 domain and thereby regulates its guanine exchange activity. | ||
| - | + | C-terminal motif within Sec7 domain regulates guanine nucleotide exchange activity via tuning protein conformation.,Qiu B, Zhang K, Wang S, Sun F Biochem Biophys Res Commun. 2014 Mar 28;446(1):380-6. doi:, 10.1016/j.bbrc.2014.02.125. Epub 2014 Mar 5. PMID:24613384<ref>PMID:24613384</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4oiy" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Qiu B]] | ||
| + | [[Category: Sun F]] | ||
| + | [[Category: Zhang K]] | ||
Current revision
Crystal structure of Sec7p catalytic domain
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