4J79

Crystal structure of beta'-COP/PEDVspike complex

4J79 の概要

• エントリーDOI: 10.2210/pdb4j79/pdb
• 関連するPDBエントリー: 4J73 4J77 4J78 4J81 4J82 4J84 4J86 4J87 4J8B 4J8G
• 分子名称: Coatomer subunit beta', Spike glycoprotein (3 entities in total)
• 機能のキーワード: sec27, beta propeller domain, er retrieval signal, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Cytoplasm (By similarity): P41811; Virion membrane; Single-pass type I membrane protein (By similarity): Q91AV1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 35048.53

構造登録者

Ma, W.,Goldberg, J. (登録日: 2013-02-12, 公開日: 2013-03-27, 最終更新日: 2024-02-28)

主引用文献

Ma, W.,Goldberg, J.
Rules for the recognition of dilysine retrieval motifs by coatomer.
Embo J., 32:926-937, 2013

PubMed Abstract: Cytoplasmic dilysine motifs on transmembrane proteins are captured by coatomer α-COP and β'-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 α-COP and β'-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 α-COP and β'-COP have generally the same specificity for KKxx and KxKxx, but only β'-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.

PubMed: 23481256
DOI: 10.1038/emboj.2013.41

実験手法

X-RAY DIFFRACTION (1.559 Å)