5nzs

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==The structure of the COPI coat leaf in complex with the ArfGAP2 uncoating factor==
==The structure of the COPI coat leaf in complex with the ArfGAP2 uncoating factor==
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<StructureSection load='5nzs' size='340' side='right' caption='[[5nzs]], [[Resolution|resolution]] 10.10&Aring;' scene=''>
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<SX load='5nzs' size='340' side='right' viewer='molstar' caption='[[5nzs]], [[Resolution|resolution]] 10.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5nzs]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NZS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NZS FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5nzs]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus], [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] and [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NZS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NZS FirstGlance]. <br>
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</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=5nzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nzs OCA], [http://pdbe.org/5nzs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nzs RCSB], [http://www.ebi.ac.uk/pdbsum/5nzs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nzs ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 10.1&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5nzs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nzs OCA], [https://pdbe.org/5nzs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nzs RCSB], [https://www.ebi.ac.uk/pdbsum/5nzs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nzs ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/COPG1_MOUSE COPG1_MOUSE]] 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 (By similarity). 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.<ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/COPB2_MOUSE COPB2_MOUSE]] 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 (By similarity). This coatomer complex protein, essential for Golgi budding and vesicular trafficking, is a selective binding protein (RACK) for protein kinase C, epsilon type. It binds to Golgi membranes in a GTP-dependent manner. [[http://www.uniprot.org/uniprot/COPZ1_MOUSE COPZ1_MOUSE]] 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 (By similarity). The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex. [[http://www.uniprot.org/uniprot/COPB_MOUSE COPB_MOUSE]] 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. Involved in the Golgi disassembly and reassembly processes during cell cycle. Involved in autophagy by playing a role in early endosome function. Plays a role in organellar compartmentalization of secretory compartments including endoplasmic reticulum (ER)-Golgi intermediate compartment (ERGIC), Golgi, trans-Golgi network (TGN) and recycling endosomes, and in biosynthetic transport of CAV1 (By similarity). Plays a functional role in facilitating the transport of kappa-type opioid receptor mRNAs into axons and enhances translation of these proteins in cortical neurons. 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.<ref>PMID:17698811</ref> <ref>PMID:19067489</ref> [[http://www.uniprot.org/uniprot/ARFG2_RAT ARFG2_RAT]] GTPase-activating protein (GAP) for ADP ribosylation factor 1 (ARF1). May regulate coatomer-mediated protein transport from the Golgi complex to the endoplasmic reticulum. Hydrolysis of ARF1-bound GTP may lead to dissociation of coatomer from Golgi-derived membranes to allow fusion with target membranes (By similarity). [[http://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE]] 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 (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity). [[http://www.uniprot.org/uniprot/COPD_MOUSE COPD_MOUSE]] 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 (By similarity). [[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>
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[https://www.uniprot.org/uniprot/COPA_MOUSE COPA_MOUSE] 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 (By similarity). Xenin stimulates exocrine pancreatic secretion. It inhibits pentagastrin-stimulated secretion of acid, to induce exocrine pancreatic secretion and to affect small and large intestinal motility. In the gut, xenin interacts with the neurotensin receptor (By similarity).
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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</div>
</div>
<div class="pdbe-citations 5nzs" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 5nzs" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Coatomer 3D structures|Coatomer 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
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</StructureSection>
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</SX>
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[[Category: Aderhold, P]]
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[[Category: Large Structures]]
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[[Category: Briggs, J A.G]]
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[[Category: Mus musculus]]
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[[Category: Dodonova, S O]]
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[[Category: Rattus norvegicus]]
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[[Category: Ganeva, I]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Hagen, W J.H]]
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[[Category: Aderhold P]]
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[[Category: Kopp, J]]
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[[Category: Briggs JAG]]
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[[Category: Roehling, S]]
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[[Category: Dodonova SO]]
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[[Category: Sinning, I]]
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[[Category: Ganeva I]]
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[[Category: Wieland, F]]
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[[Category: Hagen WJH]]
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[[Category: Arfgap2]]
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[[Category: Kopp J]]
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[[Category: Coated vesicle]]
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[[Category: Roehling S]]
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[[Category: Copi]]
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[[Category: Sinning I]]
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[[Category: Transport protein]]
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[[Category: Wieland F]]

Current revision

The structure of the COPI coat leaf in complex with the ArfGAP2 uncoating factor

5nzs, resolution 10.10Å

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OCA

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