4CSP

Structure of the F306C mutant of nitrite reductase from Achromobacter xylosoxidans

4CSP の概要

• エントリーDOI: 10.2210/pdb4csp/pdb
• 関連するPDBエントリー: 4CSZ
• 分子名称: DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, COPPER (II) ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: oxidoreductase, electron transfer, microbial atp-generating respiratory dentrification pathway
• 由来する生物種: ACHROMOBACTER XYLOSOXIDANS
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 73899.25

構造登録者

Leferink, N.G.H.,Antonyuk, S.V.,Houwman, J.A.,Scrutton, N.S.,REady, R.,Hasnain, S.S. (登録日: 2014-03-09, 公開日: 2014-07-30, 最終更新日: 2023-12-20)

主引用文献

Leferink, N.G.H.,Antonyuk, S.V.,Houwman, J.A.,Scrutton, N.S.,Eady, R.R.,Hasnain, S.S.
Impact of Residues Remote from the Catalytic Centre on Enzyme Catalysis of Copper Nitrite Reductase.
Nat.Commun., 5:4395-, 2014

PubMed Abstract: Enzyme mechanisms are often probed by structure-informed point mutations and measurement of their effects on enzymatic properties to test mechanistic hypotheses. In many cases, the challenge is to report on complex, often inter-linked elements of catalysis. Evidence for long-range effects on enzyme mechanism resulting from mutations remains sparse, limiting the design/redesign of synthetic catalysts in a predictable way. Here we show that improving the accessibility of the active site pocket of copper nitrite reductase by mutation of a surface-exposed phenylalanine residue (Phe306), located 12 Å away from the catalytic site type-2 Cu (T2Cu), profoundly affects intra-molecular electron transfer, substrate-binding and catalytic activity. Structures and kinetic studies provide an explanation for the lower affinity for the substrate and the alteration of the rate-limiting step in the reaction. Our results demonstrate that distant residues remote from the active site can have marked effects on enzyme catalysis, by driving mechanistic change through relatively minor structural perturbations.

PubMed: 25022223
DOI: 10.1038/NCOMMS5395

実験手法

X-RAY DIFFRACTION (1.7 Å)