View source for 2ynp


==yeast betaprime COP 1-604 with KTKTN motif==
<StructureSection load='2ynp' size='340' side='right'caption='[[2ynp]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ynp]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YNP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YNP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.962&#8491;</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=2ynp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ynp OCA], [https://pdbe.org/2ynp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ynp RCSB], [https://www.ebi.ac.uk/pdbsum/2ynp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ynp ProSAT]</span></td></tr>
</table>
== Function ==
[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 ==
COPI mediates retrograde trafficking from the Golgi to the endoplasmic reticulum (ER) and within the Golgi stack, sorting transmembrane proteins bearing C-terminal KKxx or KxKxx motifs. The structure of KxKxx motifs bound to the N-terminal WD-repeat domain of beta'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the beta'-COP propeller. An absolute requirement of a two-residue spacing between the terminal carboxylate group and first lysine residue results from interactions of carbonyl groups in the motif backbone with basic side chains of beta'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous alpha-COP domain. Mutation of key interacting residues in either domain or in their cognate motifs abolishes in vitro binding and results in mistrafficking of dilysine-containing cargo in yeast without compromising cell viability. Flexibility between beta'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.

Molecular Basis for Recognition of Dilysine Trafficking Motifs by COPI.,Jackson LP, Lewis M, Kent HM, Edeling MA, Evans PR, Duden R, Owen DJ Dev Cell. 2012 Nov 20. pii: S1534-5807(12)00480-7. doi:, 10.1016/j.devcel.2012.10.017. PMID:23177648<ref>PMID:23177648</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ynp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Coatomer 3D structures|Coatomer 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Synthetic construct]]
[[Category: Duden R]]
[[Category: Edeling MA]]
[[Category: Evans PR]]
[[Category: Jackson LP]]
[[Category: Kent HM]]
[[Category: Lewis M]]
[[Category: Owen DJ]]