1NIB

THE STRUCTURE OF CU-NITRITE REDUCTASE FROM ACHROMOBACTER CYCLOCLASTES AT FIVE PH VALUES, WITH NITRITE BOUND AND WITH TYPE II CU DEPLETED

1NIB の概要

• エントリーDOI: 10.2210/pdb1nib/pdb
• 関連するPDBエントリー: 1NIA 1NIC 1NID 1NIE 1NIF 2NRD
• 分子名称: NITRITE REDUCTASE, COPPER (II) ION (3 entities in total)
• 機能のキーワード: oxidoreductase (nitric oxide(a))
• 由来する生物種: Achromobacter cycloclastes
• 細胞内の位置: Periplasm: P25006
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 111560.70

構造登録者

Adman, E.T.,Godden, J.W.,Turley, S. (登録日: 1995-07-03, 公開日: 1995-12-07, 最終更新日: 2024-02-14)

主引用文献

Adman, E.T.,Godden, J.W.,Turley, S.
The structure of copper-nitrite reductase from Achromobacter cycloclastes at five pH values, with NO2- bound and with type II copper depleted.
J.Biol.Chem., 270:27458-27474, 1995

PubMed Abstract: High resolution x-ray crystallographic structures of nitrite reductase from Achromobacter cycloclastes, undertaken in order to understand the pH optimum of the reaction with nitrite, show that at pH 5.0, 5.4, 6.0, 6.2, and 6.8, no significant changes occur, other than in the occupancy of the type II copper at the active site. An extensive network of hydrogen bonds, both within and between subunits of the trimer, maintains the rigidity of the protein structure. A water occupies a site approximately 1.5 A from the site of the type II copper in the structure of the type II copper-depleted structure (at pH 5.4), again with no other significant changes in structure. In nitrite-soaked crystals, nitrite binds via its oxygens to the type II copper and replaces the water normally bound to the type II copper. The active-site cavity of the protein is distinctly hydrophobic on one side and hydrophilic on the other, providing a possible path for diffusion of the product NO. Asp-98 exhibits thermal parameter values higher than its surroundings, suggesting a role in shuttling the two protons necessary for the overall reaction. The strong structural homology with cupredoxins is described.

PubMed: 7499203
DOI: 10.1074/jbc.270.46.27458

実験手法

X-RAY DIFFRACTION (2.7 Å)