4q66

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'''Unreleased structure'''
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==Structure of Exomer bound to Arf1.==
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<StructureSection load='4q66' size='340' side='right' caption='[[4q66]], [[Resolution|resolution]] 3.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4q66]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q66 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4gns|4gns]], [[4in3|4in3]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q66 RCSB], [http://www.ebi.ac.uk/pdbsum/4q66 PDBsum]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/ARF1_YEAST ARF1_YEAST]] GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Recruits polyadenylate-binding protein PAB1 to COPI vesicles, and this is required for correct localization of the asymmetrically distributed ASH1 mRNA.<ref>PMID:15356266</ref> [[http://www.uniprot.org/uniprot/BCH1_YEAST BCH1_YEAST]] Member of the CHS5-ARF1P-binding proteins (CHAPS) which mediates export of specific cargo proteins, including chitin synthase CHS3.<ref>PMID:16498409</ref> <ref>PMID:17000877</ref> <ref>PMID:16855022</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Cargo adaptor subunits of vesicle coat protein complexes sort transmembrane proteins to distinct membrane compartments in eukaryotic cells. The exomer complex is the only cargo adaptor known to sort proteins at the trans-Golgi network into secretory vesicles. Exomer function is regulated by the Arf1 GTPase, a master regulator of trafficking at the Golgi. We report the structure of exomer bound to two copies of Arf1. Exomer interacts with each Arf1 molecule via two surfaces, one of which is a noncanonical interface that regulates GTP hydrolysis. The structure uncovers an unexpected membrane-proximal hydrophobic element that exomer uses in cooperation with Arf1 to remodel membranes. Given the constrained motion of the exomer hinge region, we envision that exomer dynamically positions multiple membrane insertion elements to drive membrane fission. In contrast to other known cargo adaptors, exomer therefore couples two functions, cargo sorting and membrane fission, into a single complex.
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The entry 4q66 is ON HOLD until Paper Publication
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Structural basis for membrane binding and remodeling by the exomer secretory vesicle cargo adaptor.,Paczkowski JE, Fromme JC Dev Cell. 2014 Sep 8;30(5):610-24. doi: 10.1016/j.devcel.2014.07.014. PMID:25203211<ref>PMID:25203211</ref>
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Authors: Paczkowski, J.E., Fromme, J.C.
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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Description: Structure of Exomer bound to Arf1.
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Fromme, J C]]
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[[Category: Paczkowski, J E]]
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[[Category: Cargo adaptor]]
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[[Category: Protein transport]]
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[[Category: Secretory vesicle]]
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[[Category: Small gtp-ase arf1-binding]]
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[[Category: Trans-golgi network]]

Revision as of 09:28, 31 December 2014

Structure of Exomer bound to Arf1.

4q66, resolution 3.35Å

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