6XA0

Crystal structure of C-As lyase with mutation K105R with Ni(II)

6XA0 の概要

• エントリーDOI: 10.2210/pdb6xa0/pdb
• 分子名称: Glyoxalase/bleomycin resistance protein/dioxygenase, NICKEL (II) ION (3 entities in total)
• 機能のキーワード: c-as lyase, oxidoreductase
• 由来する生物種: Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / NBRC 15933 / NCIMB 10081 / Henssen B9)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27079.58

構造登録者

Venkadesh, S.,Yoshinaga, M.,Kandavelu, P.,Sankaran, B.,Rosen, B.P. (登録日: 2020-06-03, 公開日: 2021-06-09, 最終更新日: 2023-10-18)

主引用文献

Nadar, V.S.,Kandavelu, P.,Sankaran, B.,Rosen, B.P.,Yoshinaga, M.
The ArsI C-As lyase: Elucidating the catalytic mechanism of degradation of organoarsenicals.
J.Inorg.Biochem., 232:111836-111836, 2022

PubMed Abstract: Organoarsenicals such as monosodium methylarsenate (MSMA or MAs(V)) and roxarsone (4-hydroxyl-3-nitrophenylarsenate or Rox(V)) have been extensively used as herbicides and growth enhancers for poultry, respectively. Degradation of organoarsenicals to inorganic arsenite (As(III)) contaminates crops and drinking water. One such process is catalyzed by the bacterial enzyme ArsI, whose gene is found in many soil bacteria. ArsI is a non-heme ferrous iron (Fe(II))-dependent dioxygenase that catalyzes oxygen-dependent cleavage of the carbon‑arsenic (C-As) bond in trivalent organoarsenicals, degrading them to inorganic As(III). From previous crystal structures of ArsI, we predicted that a loop-gating mechanism controls the catalytic reaction. Understanding the catalytic mechanism of ArsI requires knowledge of the mechanisms of substrate binding and activation of dioxygen. Here we report new ArsI structures with bound Rox(III) and mutant enzymes with alteration of active site residues. Our results elucidate steps in the catalytic cycle of this novel dioxygenase and enhance understanding of the recycling of environmental organoarsenicals.

PubMed: 35487149
DOI: 10.1016/j.jinorgbio.2022.111836

実験手法

X-RAY DIFFRACTION (2.15 Å)