2yno

yeast betaprime COP 1-304H6yeast betaprime COP 1-304H6

Structural highlights 2yno is a 3 chain structure with sequence from Saccharomyces cerevisiae and Unidentified. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2ynn, 2ynp Resources: FirstGlance, OCA, RCSB, PDBsum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 2yno, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image