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5nzr

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==The structure of the COPI coat leaf==
==The structure of the COPI coat leaf==
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<StructureSection load='5nzr' size='340' side='right' caption='[[5nzr]], [[Resolution|resolution]] 9.20&Aring;' scene=''>
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<SX load='5nzr' size='340' side='right' viewer='molstar' caption='[[5nzr]], [[Resolution|resolution]] 9.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5nzr]] is a 11 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NZR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NZR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5nzr]] is a 11 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] 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=5NZR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NZR 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=5nzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nzr OCA], [http://pdbe.org/5nzr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nzr RCSB], [http://www.ebi.ac.uk/pdbsum/5nzr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nzr 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]] 9.2&#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=5nzr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nzr OCA], [https://pdbe.org/5nzr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5nzr RCSB], [https://www.ebi.ac.uk/pdbsum/5nzr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5nzr 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/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/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/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/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).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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<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: Saccharomyces cerevisiae]]
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[[Category: Ganeva, I]]
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[[Category: Aderhold P]]
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[[Category: Hagen, W J.H]]
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[[Category: Briggs JAG]]
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[[Category: Kopp, J]]
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[[Category: Dodonova SO]]
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[[Category: Roehling, S]]
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[[Category: Ganeva I]]
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[[Category: Sinning, I]]
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[[Category: Hagen WJH]]
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[[Category: Wieland, F]]
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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: Coatomer]]
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[[Category: Sinning I]]
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[[Category: Copi]]
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[[Category: Wieland F]]
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[[Category: Transport protein]]
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Current revision

The structure of the COPI coat leaf

5nzr, resolution 9.20Å

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