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3TB3

Crystal structure of the UCH domain of UCH-L5 with 6 residues deleted

3SQA」から置き換えられました
3TB3 の概要
エントリーDOI10.2210/pdb3tb3/pdb
分子名称Ubiquitin carboxyl-terminal hydrolase isozyme L5, CALCIUM ION (3 entities in total)
機能のキーワードuch domain, hydrolase
由来する生物種Homo sapiens (human)
細胞内の位置Cytoplasm : Q9Y5K5
タンパク質・核酸の鎖数2
化学式量合計51445.92
構造登録者
Zhou, Z.R.,Zha, M.,Zhou, J.,Hu, H.Y. (登録日: 2011-08-05, 公開日: 2012-02-22, 最終更新日: 2023-11-01)
主引用文献Zhou, Z.R.,Zhang, Y.H.,Liu, S.,Song, A.X.,Hu, H.Y.
Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains.
Biochem.J., 441:143-149, 2012
Cited by
PubMed Abstract: UCHs [Ub (ubiquitin) C-terminal hydrolases] are a family of deubiquitinating enzymes that are often thought to only remove small C-terminal peptide tails from Ub adducts. Among the four UCHs identified to date, neither UCH-L3 nor UCH-L1 can catalyse the hydrolysis of isopeptide Ub chains, but UCH-L5 can when it is present in the PA700 complex of the proteasome. In the present paper, we report that the UCH domain of UCH-L5, different from UCH-L1 and UCH-L3, by itself can process the K48-diUb (Lys48-linked di-ubiquitin) substrate by cleaving the isopeptide bond between two Ub units. The catalytic specificity of the four UCHs is dependent on the length of the active-site crossover loop. The UCH domain with a long crossover loop (usually >14 residues), such as that of UCH-L5 or BAP1 [BRCA1 (breast cancer early-onset 1)-associated protein 1], is able to cleave both small and large Ub derivatives, whereas the one with a short loop can only process small Ub derivatives. We also found that elongation of the crossover loop enables UCH-L1 to have isopeptidase activity for K48-diUb in a length-dependent manner. Thus the loop length of UCHs defines their substrate specificity for diUb chains, suggesting that the chain flexibility of the crossover loop plays an important role in determining its catalytic activity and substrate specificity for cleaving isopeptide Ub chains.
PubMed: 21851340
DOI: 10.1042/BJ20110699
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.3 Å)
構造検証レポート
Validation report summary of 3tb3
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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