3A7S

Catalytic domain of UCH37

3A7S の概要

• エントリーDOI: 10.2210/pdb3a7s/pdb
• 分子名称: Ubiquitin carboxyl-terminal hydrolase isozyme L5, CHLORIDE ION (3 entities in total)
• 機能のキーワード: ubiquitin-proteasome pathway, alternative splicing, hydrolase, polymorphism, protease, proteasome, thiol protease, ubl conjugation pathway
• 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: 1
• 化学式量合計: 25703.39

構造登録者

Nishio, K.,Kim, S.W.,Kawai, K.,Mizushima, T.,Yamane, T.,Hamazaki, J.,Murata, S.,Tanaka, K. (登録日: 2009-10-04, 公開日: 2009-11-03, 最終更新日: 2024-05-29)

主引用文献

Nishio, K.,Kim, S.W.,Kawai, K.,Mizushima, T.,Yamane, T.,Hamazaki, J.,Murata, S.,Tanaka, K.,Morimoto, Y.
Crystal structure of the de-ubiquitinating enzyme UCH37 (human UCH-L5) catalytic domain
Biochem.Biophys.Res.Commun., 2009

PubMed Abstract: Ubiquitin C-terminal hydrolases (UCHs) are one of five sub-families of de-ubiquitinating enzymes (DUBs) that hydrolyze the C-terminal peptide bond of ubiquitin. UCH37 (also called UCH-L5) is the only UCH family protease that interacts with the 19S proteasome regulatory complex and disassembles Lys48-linked poly-ubiquitin from the distal end of the chain. The structures of three UCHs, UCH-L1, UCH-L3, and YUH1, have been determined by X-ray crystallography. However, little is known about their physiological substrates. These enzymes do not hydrolyze large adducts of ubiquitin such as proteins. To identify and characterize the hydrolytic specificities of their substrates, the crystal structure of the UCH37 catalytic domain (UCH-domain) was determined and compared with that of the other UCHs. The overall folding patterns are similar in these UCHs. However, helix-3 is collapsed in UCH37 and the pattern of electrostatic potential on the surface of the putative substrate-binding site (P'-site) is different. Helix-3 comprises an edge of the P'-site. As a result, the P'-site is wider than that in other UCHs. These differences indicate that UCH37 can interact with larger adducts such as ubiquitin.

PubMed: 19836345
DOI: 10.1016/j.bbrc.2009.10.062

実験手法

X-RAY DIFFRACTION (2.2 Å)