5SYK

Crystal structure of B. pseudomallei KatG treated with hydrogen peroxide

「4MVP」から置き換えられました

5SYK の概要

• エントリーDOI: 10.2210/pdb5syk/pdb
• 分子名称: Catalase-peroxidase, PROTOPORPHYRIN IX CONTAINING FE, SODIUM ION, ... (8 entities in total)
• 機能のキーワード: catalase-peroxidase, katg, hydrogen peroxide, oxidreductase, inh, oxidoreductase
• 由来する生物種: Burkholderia pseudomallei (strain 1710b)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 160788.17

構造登録者

Loewen, P.C. (登録日: 2016-08-11, 公開日: 2016-09-21, 最終更新日: 2023-11-15)

主引用文献

Loewen, P.C.,Carpena, X.,Vidossich, P.,Fita, I.,Rovira, C.
An ionizable active-site tryptophan imparts catalase activity to a peroxidase core.
J. Am. Chem. Soc., 136:7249-7252, 2014

PubMed Abstract: Catalase peroxidases (KatG's) are bifunctional heme proteins that can disproportionate hydrogen peroxide (catalatic reaction) despite their structural dissimilarity with monofunctional catalases. Using X-ray crystallography and QM/MM calculations, we demonstrate that the catalatic reaction of KatG's involves deprotonation of the active-site Trp, which plays a role similar to that of the distal His in monofunctional catalases. The interaction of a nearby mobile arginine with the distal Met-Tyr-Trp essential adduct (in/out) acts as an electronic switch, triggering deprotonation of the adduct Trp.

PubMed: 24785434
DOI: 10.1021/ja502794e

実験手法

X-RAY DIFFRACTION (1.8 Å)