3tjz
From Proteopedia
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| - | [[ | + | ==Crystal Structure of Arf1 Bound to the gamma/zeta-COP Core Complex== |
| + | <StructureSection load='3tjz' size='340' side='right' caption='[[3tjz]], [[Resolution|resolution]] 2.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3tjz]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TJZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TJZ FirstGlance]. <br> | ||
| + | </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> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ARF1, YDL192W, D1244 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]), COPG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus]), COPZ1, COPZ ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 Bos taurus])</td></tr> | ||
| + | <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=3tjz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tjz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tjz RCSB], [http://www.ebi.ac.uk/pdbsum/3tjz PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[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/COPG_BOVIN COPG_BOVIN]] The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated to ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors. Required for limiting lipid storage in lipid droplets. Involved in lipid homeostasis by regulating the presence of perilipin family members PLIN2 and PLIN3 at the lipid droplet surface and promoting the association of adipocyte triglyceride lipase (PNPLA2) with the lipid droplet surface to mediate lipolysis (By similarity). | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Budding of COPI-coated vesicles from Golgi membranes requires an Arf family G protein and the coatomer complex recruited from cytosol. Arf is also required with coatomer-related clathrin adaptor complexes to bud vesicles from the trans-Golgi network and endosomal compartments. To understand the structural basis for Arf-dependent recruitment of a vesicular coat to the membrane, we determined the structure of Arf1 bound to the gammazeta-COP subcomplex of coatomer. Structure-guided biochemical analysis reveals that a second Arf1-GTP molecule binds to betadelta-COP at a site common to the gamma- and beta-COP subunits. The Arf1-binding sites on coatomer are spatially related to PtdIns4,5P(2)-binding sites on the endocytic AP2 complex, providing evidence that the orientation of membrane binding is general for this class of vesicular coat proteins. A bivalent GTP-dependent binding mode has implications for the dynamics of coatomer interaction with the Golgi and for the selection of cargo molecules. | ||
| - | + | A structure-based mechanism for arf1-dependent recruitment of coatomer to membranes.,Yu X, Breitman M, Goldberg J Cell. 2012 Feb 3;148(3):530-42. PMID:22304919<ref>PMID:22304919</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Breitman, M | + | [[Category: Breitman, M]] |
| - | [[Category: Goldberg, J | + | [[Category: Goldberg, J]] |
| - | [[Category: Yu, X | + | [[Category: Yu, X]] |
[[Category: Golgi membrane]] | [[Category: Golgi membrane]] | ||
[[Category: Protein trafficking]] | [[Category: Protein trafficking]] | ||
[[Category: Protein transport-protein binding complex]] | [[Category: Protein transport-protein binding complex]] | ||
Revision as of 11:20, 25 December 2014
Crystal Structure of Arf1 Bound to the gamma/zeta-COP Core Complex
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