3A55

Crystal structure of the A47Q2 mutant of pro- protein-glutaminase

3A55 の概要

• エントリーDOI: 10.2210/pdb3a55/pdb
• 関連するPDBエントリー: 2ZK9 3A54 3A56
• 分子名称: Protein-glutaminase (2 entities in total)
• 機能のキーワード: mutant structure like the reaction intermediate, hydrolase
• 由来する生物種: Chryseobacterium proteolyticum
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 67223.50

構造登録者

Hashizume, R.,Yamaguchi, S.,Mikami, B. (登録日: 2009-07-30, 公開日: 2010-08-11, 最終更新日: 2024-11-06)

主引用文献

Hashizume, R.,Maki, Y.,Mizutani, K.,Takahashi, N.,Matsubara, H.,Sugita, A.,Sato, K.,Yamaguchi, S.,Mikami, B.
Crystal structures of protein glutaminase and its pro forms converted into enzyme-substrate complex
J.Biol.Chem., 286:38691-38702, 2011

PubMed Abstract: Protein glutaminase, which converts a protein glutamine residue to a glutamate residue, is expected to be useful as a new food-processing enzyme. The crystal structures of the mature and pro forms of the enzyme were refined at 1.15 and 1.73 Å resolution, respectively. The overall structure of the mature enzyme has a weak homology to the core domain of human transglutaminase-2. The catalytic triad (Cys-His-Asp) common to transglutaminases and cysteine proteases is located in the bottom of the active site pocket. The structure of the recombinant pro form shows that a short loop between S2 and S3 in the proregion covers and interacts with the active site of the mature region, mimicking the protein substrate of the enzyme. Ala-47 is located just above the pocket of the active site. Two mutant structures (A47Q-1 and A47Q-2) refined at 1.5 Å resolution were found to correspond to the enzyme-substrate complex and an S-acyl intermediate. Based on these structures, the catalytic mechanism of protein glutaminase is proposed.

PubMed: 21926168
DOI: 10.1074/jbc.M111.255133

実験手法

X-RAY DIFFRACTION (1.5 Å)