2BO0

Crystal structure of the C130A mutant of nitrite reductase from Alcaligenes xylosoxidans

2BO0 の概要

• エントリーDOI: 10.2210/pdb2bo0/pdb
• 関連するPDBエントリー: 1BQ5 1GS6 1GS7 1GS8 1HAU 1HAW 1NDT 1OE1 1OE2 1OE3 1WA0 1WA1 1WA2 1WAE
• 分子名称: DISSIMILATORY COPPER-CONTAINING NITRITE REDUCTASE, ZINC ION, TETRAETHYLENE GLYCOL, ... (4 entities in total)
• 機能のキーワード: denitrification, nitrite reductase, c130a, mutant, electron transfer, oxidoreductase, copper, fad, flavoprotein, metal- binding, nitrate assimilation, periplasmic
• 由来する生物種: ACHROMOBACTER XYLOSOXIDANS
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 36911.88

構造登録者

Hough, M.A.,Ellis, M.J.,Antonyuk, S.,Strange, R.W.,Sawers, G.,Eady, R.R.,Hasnain, S.S. (登録日: 2005-04-06, 公開日: 2006-10-18, 最終更新日: 2024-11-20)

主引用文献

Hough, M.A.,Ellis, M.J.,Antonyuk, S.,Strange, R.W.,Sawers, G.,Eady, R.R.,Hasnain, S.S.
High Resolution Structural Studies of Mutants Provide Insights Into Catalysis and Electron Transfer Processes in Copper Nitrite Reductase
J.Mol.Biol., 350:300-, 2005

PubMed Abstract: We present high-resolution crystal structures and functional analysis of T1Cu centre mutants of nitrite reductase that perturb the redox potential and the Cys130-His129 "hard-wired" bridge through which electron transfer to the catalytic T2Cu centre occurs. These data provide insight into how activity can be altered through mutational manipulation of the electron delivery centre (T1Cu). The alteration of Cys to Ala results in loss of T1Cu and enzyme inactivation with azurin as electron donor despite the mutant enzyme retaining full nitrite-binding capacity. These data establish unequivocally that no direct transfer of electrons occurs from azurin to the catalytic type 2 Cu centre. The mutation of the axial ligand Met144 to Leu increases both the redox potential and catalytic activity, establishing that the rate-determining step of catalysis is the intermolecular electron transfer from azurin to nitrite reductase.

PubMed: 15927201
DOI: 10.1016/J.JMB.2005.04.006

実験手法

X-RAY DIFFRACTION (1.35 Å)