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| | <StructureSection load='4j8b' size='340' side='right'caption='[[4j8b]], [[Resolution|resolution]] 1.88Å' scene=''> | | <StructureSection load='4j8b' size='340' side='right'caption='[[4j8b]], [[Resolution|resolution]] 1.88Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4j8b]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J8B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J8B FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4j8b]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe Schizosaccharomyces pombe]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J8B FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j73|4j73]], [[4j77|4j77]], [[4j78|4j78]], [[4j79|4j79]], [[4j81|4j81]], [[4j82|4j82]], [[4j84|4j84]], [[4j86|4j86]], [[4j87|4j87]], [[4j8g|4j8g]]</td></tr> | + | </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=4j8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j8b OCA], [https://pdbe.org/4j8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j8b RCSB], [https://www.ebi.ac.uk/pdbsum/4j8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j8b ProSAT]</span></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=4j8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j8b OCA], [http://pdbe.org/4j8b PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j8b RCSB], [http://www.ebi.ac.uk/pdbsum/4j8b PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j8b ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/COPA_SCHPO COPA_SCHPO]] 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). | + | [https://www.uniprot.org/uniprot/COPA_SCHPO COPA_SCHPO] 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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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| | + | [[Category: Saccharomyces cerevisiae]] |
| | [[Category: Schizosaccharomyces pombe]] | | [[Category: Schizosaccharomyces pombe]] |
| - | [[Category: Goldberg, J]] | + | [[Category: Goldberg J]] |
| - | [[Category: Ma, W]] | + | [[Category: Ma W]] |
| - | [[Category: Beta propeller domain]]
| + | |
| - | [[Category: Dilysine motif]]
| + | |
| - | [[Category: Er retrieval]]
| + | |
| - | [[Category: Protein transport]]
| + | |
| Structural highlights
Function
COPA_SCHPO 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
Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer alpha-COP and beta'-COP subunits and packaged into COPI-coated vesicles for Golgi-to-ER retrieval. Numerous ER/Golgi proteins contain K(x)Kxx motifs, but the rules for their recognition are unclear. We present crystal structures of alpha-COP and beta'-COP bound to a series of naturally occurring retrieval motifs-encompassing KKxx, KxKxx and non-canonical RKxx and viral KxHxx sequences. Binding experiments show that alpha-COP and beta'-COP have generally the same specificity for KKxx and KxKxx, but only beta'-COP recognizes the RKxx signal. Dilysine motif recognition involves lysine side-chain interactions with two acidic patches. Surprisingly, however, KKxx and KxKxx motifs bind differently, with their lysine residues transposed at the binding patches. We derive rules for retrieval motif recognition from key structural features: the reversed binding modes, the recognition of the C-terminal carboxylate group which enforces lysine positional context, and the tolerance of the acidic patches for non-lysine residues.
Rules for the recognition of dilysine retrieval motifs by coatomer.,Ma W, Goldberg J EMBO J. 2013 Mar 12. doi: 10.1038/emboj.2013.41. PMID:23481256[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ma W, Goldberg J. Rules for the recognition of dilysine retrieval motifs by coatomer. EMBO J. 2013 Mar 12. doi: 10.1038/emboj.2013.41. PMID:23481256 doi:http://dx.doi.org/10.1038/emboj.2013.41
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