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| | ==Crystal Structure of the beta/delta-COPI Core Complex== | | ==Crystal Structure of the beta/delta-COPI Core Complex== |
| - | <StructureSection load='5mu7' size='340' side='right' caption='[[5mu7]], [[Resolution|resolution]] 2.57Å' scene=''> | + | <StructureSection load='5mu7' size='340' side='right'caption='[[5mu7]], [[Resolution|resolution]] 2.57Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mu7]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Chatd Chatd]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MU7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MU7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mu7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chaetomium_thermophilum_var._thermophilum_DSM_1495 Chaetomium thermophilum var. thermophilum DSM 1495]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MU7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MU7 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CTHT_0034860 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD]), CTHT_0026330 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=759272 CHATD])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.57Å</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=5mu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mu7 OCA], [http://pdbe.org/5mu7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mu7 RCSB], [http://www.ebi.ac.uk/pdbsum/5mu7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mu7 ProSAT]</span></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=5mu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mu7 OCA], [https://pdbe.org/5mu7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mu7 RCSB], [https://www.ebi.ac.uk/pdbsum/5mu7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mu7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/G0S6G7_CHATD G0S6G7_CHATD]] 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.[PIRNR:PIRNR005727] [[http://www.uniprot.org/uniprot/G0S6I4_CHATD G0S6I4_CHATD]] 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.[RuleBase:RU364018] | + | [https://www.uniprot.org/uniprot/G0S6G7_CHATD G0S6G7_CHATD] 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.[PIRNR:PIRNR005727] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Chatd]] | + | [[Category: Chaetomium thermophilum var. thermophilum DSM 1495]] |
| - | [[Category: Aderhold, P]] | + | [[Category: Large Structures]] |
| - | [[Category: Kopp, J]] | + | [[Category: Aderhold P]] |
| - | [[Category: Sinning, I]] | + | [[Category: Kopp J]] |
| - | [[Category: Wieland, F]] | + | [[Category: Sinning I]] |
| - | [[Category: Beta cop]]
| + | [[Category: Wieland F]] |
| - | [[Category: Coatomer]]
| + | |
| - | [[Category: Copi]]
| + | |
| - | [[Category: Delta cop]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
G0S6G7_CHATD 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.[PIRNR:PIRNR005727]
Publication Abstract from PubMed
COPI coated vesicles mediate trafficking within the Golgi apparatus and between the Golgi and the endoplasmic reticulum. Assembly of a COPI coated vesicle is initiated by the small GTPase Arf1 that recruits the coatomer complex to the membrane, triggering polymerization and budding. The vesicle uncoats before fusion with a target membrane. Coat components are structurally conserved between COPI and clathrin/adaptor proteins. Using cryo-electron tomography and subtomogram averaging, we determined the structure of the COPI coat assembled on membranes in vitro at 9 A resolution. We also obtained a 2.57 A resolution crystal structure of betadelta-COP. By combining these structures we built a molecular model of the coat. We additionally determined the coat structure in the presence of ArfGAP proteins that regulate coat dissociation. We found that Arf1 occupies contrasting molecular environments within the coat, leading us to hypothesize that some Arf1 molecules may regulate vesicle assembly while others regulate coat disassembly.
9A structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.,Dodonova SO, Aderhold P, Kopp J, Ganeva I, Rohling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG Elife. 2017 Jun 16;6. pii: e26691. doi: 10.7554/eLife.26691. PMID:28621666[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dodonova SO, Aderhold P, Kopp J, Ganeva I, Rohling S, Hagen WJH, Sinning I, Wieland F, Briggs JAG. 9A structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments. Elife. 2017 Jun 16;6. pii: e26691. doi: 10.7554/eLife.26691. PMID:28621666 doi:http://dx.doi.org/10.7554/eLife.26691
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