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4j77

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Crystal structure of beta'-COP/hWbp1 complex

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Retrieved from "http://52.214.119.220/wiki/index.php/4j77"

Categories: Homo sapiens | Large Structures | Saccharomyces cerevisiae | Goldberg J | Ma W

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 <StructureSection load='4j77' size='340' side='right'caption='[[4j77]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4j77]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4J77 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4J77 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4j77]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=4J77 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4J77 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4j73|4j73]], [[4j78|4j78]], [[4j79|4j79]], [[4j81|4j81]], [[4j82|4j82]], [[4j84|4j84]], [[4j86|4j86]], [[4j87|4j87]], [[4j8b|4j8b]], [[4j8g|4j8g]]</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]] 1.756&#8491;</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=4j77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j77 OCA], [http://pdbe.org/4j77 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4j77 RCSB], [http://www.ebi.ac.uk/pdbsum/4j77 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4j77 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=4j77 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4j77 OCA], [https://pdbe.org/4j77 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4j77 RCSB], [https://www.ebi.ac.uk/pdbsum/4j77 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4j77 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/COPB2_YEAST COPB2_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.<ref>PMID:17101773</ref>
+[https://www.uniprot.org/uniprot/COPB2_YEAST COPB2_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.<ref>PMID:17101773</ref>
-<div style="background-color:#fffaf0;">
-== 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<ref>PMID:23481256</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 4j77" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
 [[Category: Saccharomyces cerevisiae]]
-[[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]]

4j77

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Crystal structure of beta'-COP/hWbp1 complex

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