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1NIC

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

Summary for 1NIC
Entry DOI10.2210/pdb1nic/pdb
Related1NIA 1NIB 1NID 1NIE 1NIF 2NRD
DescriptorNITRITE REDUCTASE, COPPER (II) ION, SULFATE ION, ... (4 entities in total)
Functional Keywordsoxidoreductase (nitric oxide(a))
Biological sourceAchromobacter cycloclastes
Cellular locationPeriplasm: P25006
Total number of polymer chains1
Total formula weight37282.96
Authors
Adman, E.T.,Godden, J.W.,Turley, S. (deposition date: 1995-07-03, release date: 1995-12-07, Last modification date: 2024-02-14)
Primary citationAdman, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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