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| | ==Yeast delta-COP-I mu-homology domain complexed with Gcs1 WxxF peptide== | | ==Yeast delta-COP-I mu-homology domain complexed with Gcs1 WxxF peptide== |
| - | <StructureSection load='5fjx' size='340' side='right' caption='[[5fjx]], [[Resolution|resolution]] 2.45Å' scene=''> | + | <StructureSection load='5fjx' size='340' side='right'caption='[[5fjx]], [[Resolution|resolution]] 2.45Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5fjx]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FJX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5fjx]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FJX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FJX FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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]] 2.45Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fjw|5fjw]], [[5fjz|5fjz]], [[5fk0|5fk0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=5fjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjx OCA], [http://pdbe.org/5fjx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fjx RCSB], [http://www.ebi.ac.uk/pdbsum/5fjx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjx 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=5fjx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fjx OCA], [https://pdbe.org/5fjx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fjx RCSB], [https://www.ebi.ac.uk/pdbsum/5fjx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fjx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COPD_YEAST COPD_YEAST]] 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 (By similarity). [[http://www.uniprot.org/uniprot/GCS1_YEAST GCS1_YEAST]] GTPase-activating protein (GAP) for ARF1 and ARF2. Involved in intracellular vesicular transport. Required for transport from the trans-Golgi network. Implicated in the regulation of retrograde transport from the Golgi to the ER and in actin cytoskeletal organization. May be involved in the maintenance of mitochondrial morphology, possibly through organizing the actin cytoskeleton in Saccharomyces.<ref>PMID:11756474</ref> <ref>PMID:11839779</ref> <ref>PMID:9927415</ref> | + | [https://www.uniprot.org/uniprot/COPD_YEAST COPD_YEAST] 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 (By similarity). |
| | <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: Atcc 18824]] | + | [[Category: Large Structures]] |
| - | [[Category: Evans, P R]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Owen, D J]] | + | [[Category: Evans PR]] |
| - | [[Category: Suckling, R J]] | + | [[Category: Owen DJ]] |
| - | [[Category: Cop-i]] | + | [[Category: Suckling RJ]] |
| - | [[Category: Protein transport]]
| + | |
| - | [[Category: Vesicle coat protein]]
| + | |
| Structural highlights
Function
COPD_YEAST 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 (By similarity).
Publication Abstract from PubMed
Coatomer consists of two subcomplexes: the membrane-targeting, ADP ribosylation factor 1 (Arf1):GTP-binding betagammadeltazeta-COP F-subcomplex, which is related to the adaptor protein (AP) clathrin adaptors, and the cargo-binding alphabeta'epsilon-COP B-subcomplex. We present the structure of the C-terminal mu-homology domain of the yeast delta-COP subunit in complex with the WxW motif from its binding partner, the endoplasmic reticulum-localized Dsl1 tether. The motif binds at a site distinct from that used by the homologous AP mu subunits to bind YxxPhi cargo motifs with its two tryptophan residues sitting in compatible pockets. We also show that the Saccharomyces cerevisiae Arf GTPase-activating protein (GAP) homolog Gcs1p uses a related WxxF motif at its extreme C terminus to bind to delta-COP at the same site in the same way. Mutations designed on the basis of the structure in conjunction with isothermal titration calorimetry confirm the mode of binding and show that mammalian delta-COP binds related tryptophan-based motifs such as that from ArfGAP1 in a similar manner. We conclude that delta-COP subunits bind Wxn(1-6)[WF] motifs within unstructured regions of proteins that influence the lifecycle of COPI-coated vesicles; this conclusion is supported by the observation that, in the context of a sensitizing domain deletion in Dsl1p, mutating the tryptophan-based motif-binding site in yeast causes defects in both growth and carboxypeptidase Y trafficking/processing.
Structural basis for the binding of tryptophan-based motifs by delta-COP.,Suckling RJ, Poon PP, Travis SM, Majoul IV, Hughson FM, Evans PR, Duden R, Owen DJ Proc Natl Acad Sci U S A. 2015 Nov 17;112(46):14242-7. doi:, 10.1073/pnas.1506186112. Epub 2015 Nov 2. PMID:26578768[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Suckling RJ, Poon PP, Travis SM, Majoul IV, Hughson FM, Evans PR, Duden R, Owen DJ. Structural basis for the binding of tryptophan-based motifs by delta-COP. Proc Natl Acad Sci U S A. 2015 Nov 17;112(46):14242-7. doi:, 10.1073/pnas.1506186112. Epub 2015 Nov 2. PMID:26578768 doi:http://dx.doi.org/10.1073/pnas.1506186112
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