2XK5

Crystal structure of K6-linked diubiquitin

2XK5 の概要

• エントリーDOI: 10.2210/pdb2xk5/pdb
• 関連するPDBエントリー: 1C3T 1D3Z 1F9J 1FXT 1G6J 1GJZ 1NBF 1OGW 1Q5W 1S1Q 1SIF 1TBE 1UBI 1UBQ 1XD3 1XQQ 1YX5 1YX6 1ZGU 2AYO 2BGF 2G45 2GBJ 2GBK 2GBM 2GBN 2J7Q 2JF5 2W9N 2WDT 2XEW
• 分子名称: UBIQUITIN, ZINC ION (3 entities in total)
• 機能のキーワード: signal transduction, brca1, protein binding
• 由来する生物種: HOMO SAPIENS (HUMAN); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 17624.57

構造登録者

Virdee, S.,Chin, J.W.,Komander, D. (登録日: 2010-07-07, 公開日: 2010-08-25, 最終更新日: 2023-12-20)

主引用文献

Virdee, S.,Ye, Y.,Nguyen, D.P.,Komander, D.,Chin, J.W.
Engineered Diubiquitin Synthesis Reveals K29-Isopeptide Specificity of an Otu Deubiquitinase
Nat.Chem.Biol., 6:750-, 2010

PubMed Abstract: Ubiquitination is a reversible post-translational modification that regulates a myriad of eukaryotic functions. Our ability to study the effects of ubiquitination is often limited by the inaccessibility of homogeneously ubiquitinated proteins. In particular, elucidating the roles of the so-called 'atypical' ubiquitin chains (chains other than Lys48- or Lys63-linked ubiquitin), which account for a large fraction of ubiquitin polymers, is challenging because the enzymes for their biosynthesis are unknown. Here we combine genetic code expansion, intein chemistry and chemoselective ligations to synthesize 'atypical' ubiquitin chains. We solve the crystal structure of Lys6-linked diubiquitin, which is distinct from that of structurally characterized ubiquitin chains, providing a molecular basis for the different biological functions this linkage may regulate. Moreover, we profile a panel containing 10% of the known human deubiquitinases on Lys6- and Lys29-linked ubiquitin and discover that TRABID cleaves the Lys29 linkage 40-fold more efficiently than the Lys63 linkage.

PubMed: 20802491
DOI: 10.1038/NCHEMBIO.426

実験手法

X-RAY DIFFRACTION (3 Å)