4M5W

Crystal structure of the USP7/HAUSP catalytic domain

4M5W の概要

• エントリーDOI: 10.2210/pdb4m5w/pdb
• 関連するPDBエントリー: 4M5X
• 分子名称: Ubiquitin carboxyl-terminal hydrolase 7, BROMIDE ION (3 entities in total)
• 機能のキーワード: ubiquitin-specific cysteine protease, hydrolase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: Q93009
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 41468.09

構造登録者

Molland, K.L.,Mesecar, A.D.,Zhou, Q. (登録日: 2013-08-08, 公開日: 2014-03-12, 最終更新日: 2023-09-20)

主引用文献

Molland, K.,Zhou, Q.,Mesecar, A.D.
A 2.2 angstrom resolution structure of the USP7 catalytic domain in a new space group elaborates upon structural rearrangements resulting from ubiquitin binding.
Acta Crystallogr F Struct Biol Commun, 70:283-287, 2014

PubMed Abstract: A sparse-matrix screen for new crystallization conditions for the USP7 catalytic domain (USP7CD) led to the identification of a condition in which crystals grow reproducibly in 24-48 h. Variation of the halide metal, growth temperature and seed-stock concentration resulted in a shift in space group from P21 with two molecules in the asymmetric unit to C2 with one molecule in the asymmetric unit. Representative structures from each space group were determined to 2.2 Å resolution and these structures support previous findings that the catalytic triad and switching loop are likely to be in unproductive conformations in the absence of ubiquitin (Ub). Importantly, the new structures reveal previously unobserved electron density for blocking loop 1 (BL1) residues 410-419. The new structures indicate a distinct rearrangement of the USP7 BL1 compared with its position in the presence of bound Ub.

PubMed: 24598911
DOI: 10.1107/S2053230X14002519

実験手法

X-RAY DIFFRACTION (2.244 Å)