2N3V

Solution structure of the Rpn1 T1 site with K48-linked diubiquitin in the extended binding mode

2N3V の概要

• エントリーDOI: 10.2210/pdb2n3v/pdb
• 関連するPDBエントリー: 2N3T 2N3U 2N3W
• 分子名称: 26S proteasome regulatory subunit RPN1, Ubiquitin-60S ribosomal protein L40 (2 entities in total)
• 機能のキーワード: protein binding
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• 細胞内の位置: Ubiquitin: Cytoplasm . 60S ribosomal protein L40: Cytoplasm : P62987
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 30790.25

構造登録者

Chen, X.,Walters, K.J. (登録日: 2015-06-10, 公開日: 2016-02-24, 最終更新日: 2024-11-06)

主引用文献

Shi, Y.,Chen, X.,Elsasser, S.,Stocks, B.B.,Tian, G.,Lee, B.H.,Shi, Y.,Zhang, N.,de Poot, S.A.,Tuebing, F.,Sun, S.,Vannoy, J.,Tarasov, S.G.,Engen, J.R.,Finley, D.,Walters, K.J.
Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome.
Science, 351:-, 2016

PubMed Abstract: Hundreds of pathways for degradation converge at ubiquitin recognition by a proteasome. Here, we found that the five known proteasomal ubiquitin receptors in yeast are collectively nonessential for ubiquitin recognition and identified a sixth receptor, Rpn1. A site ( T1: ) in the Rpn1 toroid recognized ubiquitin and ubiquitin-like ( UBL: ) domains of substrate shuttling factors. T1 structures with monoubiquitin or lysine 48 diubiquitin show three neighboring outer helices engaging two ubiquitins. T1 contributes a distinct substrate-binding pathway with preference for lysine 48-linked chains. Proximal to T1 within the Rpn1 toroid is a second UBL-binding site ( T2: ) that assists in ubiquitin chain disassembly, by binding the UBL of deubiquitinating enzyme Ubp6. Thus, a two-site recognition domain intrinsic to the proteasome uses distinct ubiquitin-fold ligands to assemble substrates, shuttling factors, and a deubiquitinating enzyme.

PubMed: 26912900
DOI: 10.1126/science.aad9421

実験手法

SOLUTION NMR