1CMX

STRUCTURAL BASIS FOR THE SPECIFICITY OF UBIQUITIN C-TERMINAL HYDROLASES

1CMX の概要

• エントリーDOI: 10.2210/pdb1cmx/pdb
• 分子名称: PROTEIN (UBIQUITIN YUH1-UBAL) (3 entities in total)
• 機能のキーワード: ubiquitin hydrolase, ubiquitin, deubiquitinating enzyme, cysteine protease, enzyme specificity, hydrolase
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 69673.90

構造登録者

Johnston, S.C.,Riddle, S.M.,Cohen, R.E.,Hill, C.P. (登録日: 1999-05-12, 公開日: 1999-07-27, 最終更新日: 2023-12-27)

主引用文献

Johnston, S.C.,Riddle, S.M.,Cohen, R.E.,Hill, C.P.
Structural basis for the specificity of ubiquitin C-terminal hydrolases.
EMBO J., 18:3877-3887, 1999

PubMed Abstract: The release of ubiquitin from attachment to other proteins and adducts is critical for ubiquitin biosynthesis, proteasomal degradation and other cellular processes. De-ubiquitination is accomplished in part by members of the UCH (ubiquitin C-terminal hydrolase) family of enzymes. We have determined the 2.25 A resolution crystal structure of the yeast UCH, Yuh1, in a complex with the inhibitor ubiquitin aldehyde (Ubal). The structure mimics the tetrahedral intermediate in the reaction pathway and explains the very high enzyme specificity. Comparison with a related, unliganded UCH structure indicates that ubiquitin binding is coupled to rearrangements which block the active-site cleft in the absence of authentic substrate. Remarkably, a 21-residue loop that becomes ordered upon binding Ubal lies directly over the active site. Efficiently processed substrates apparently pass through this loop, and constraints on the loop conformation probably function to control UCH specificity.

PubMed: 10406793
DOI: 10.1093/emboj/18.14.3877

実験手法

X-RAY DIFFRACTION (2.25 Å)