2YNO

yeast betaprime COP 1-304H6

Summary for 2YNO

• Entry DOI: 10.2210/pdb2yno/pdb
• Related: 2YNN 2YNP
• Descriptor: COATOMER SUBUNIT BETA', POLY ALA (3 entities in total)
• Functional Keywords: protein transport, membrane trafficking, copi-mediated trafficking, dilysine motifs
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Cytoplasm (By similarity): P41811
• Total number of polymer chains: 3
• Total formula weight: 71335.05

Authors

Jackson, L.P.,Lewis, M.,Kent, H.M.,Edeling, M.A.,Evans, P.R.,Duden, R.,Owen, D.J. (deposition date: 2012-10-17, release date: 2012-12-12, Last modification date: 2024-05-08)

Primary citation

Jackson, L.P.,Lewis, M.,Kent, H.M.,Edeling, M.A.,Evans, P.R.,Duden, R.,Owen, D.J.
Molecular Basis for Recognition of Dilysine Trafficking Motifs by Copi.
Dev.Cell, 23:1255-, 2012

PubMed Abstract: 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 β'-COP identifies electrostatic contacts between the motif and complementary patches at the center of the β'-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 β'-COP. Similar interactions are proposed to mediate binding of KKxx motifs by the homologous α-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 β'-COP WD-repeat domains and the location of cargo binding have implications for COPI coat assembly.

PubMed: 23177648
DOI: 10.1016/J.DEVCEL.2012.10.017

Experimental method

X-RAY DIFFRACTION (1.8 Å)