2YNN

yeast betaprime COP 1-304 with KTKTN motif

2YNN の概要

• エントリーDOI: 10.2210/pdb2ynn/pdb
• 関連するPDBエントリー: 2YNO 2YNP
• 分子名称: COATOMER SUBUNIT BETA', KTKTN MOTIF, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: protein transport, peptide binding protein, membrane trafficking, copi-mediated trafficking, dilysine motifs
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P41811
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35884.25

構造登録者

Jackson, L.P.,Lewis, M.,Kent, H.M.,Edeling, M.A.,Evans, P.R.,Duden, R.,Owen, D.J. (登録日: 2012-10-17, 公開日: 2012-12-12, 最終更新日: 2024-11-06)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.782 Å)