1zv2

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Revision as of 08:33, 21 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1zv2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zv2, resolution 1.74Å" /> '''Cu-containing nitrit...)
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File:1zv2.gif


1zv2, resolution 1.74Å

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Cu-containing nitrite reductase

OverviewOverview

Nitrite reductase is an enzyme operating in the denitrification pathway, which catalyses the conversion of nitrite (NO2(-)) to gaseous nitric oxide, (NO). Here, crystal structures of the oxidized and reduced forms of the, copper-containing nitrite reductase from Rhodobacter sphaeroides 2.4.3 are, presented at 1.74 and 1.85 A resolution, respectively. Whereas the, structure of the enzyme is very similar to those of other, copper-containing nitrite reductases, folding as a trimer and containing, two copper sites per monomer, the structures reported here enable, conformational differences between the oxidized and reduced forms of the, enzyme to be identified. In the type 1 copper site, a rotational, perturbation of the side chain of the copper ligand Met182 occurs upon, reduction. At the type 2 copper site, a dual conformation of the catalytic, residue His287 is observed in the oxidized structure but is lacking in the, reduced structure, such that the interactions of the oxidized type 2, copper ion can be regarded as adopting octahedral geometry. These findings, shed light on the structural mechanism of the reduction of a copper-bound, nitrite to nitric oxide and water.

About this StructureAbout this Structure

1ZV2 is a Single protein structure of sequence from Rhodobacter sphaeroides with CU and MG as ligands. Active as Nitrite reductase (NO-forming), with EC number 1.7.2.1 Full crystallographic information is available from OCA.

ReferenceReference

Structures of the oxidized and reduced forms of nitrite reductase from Rhodobacter sphaeroides 2.4.3 at high pH: changes in the interactions of the type 2 copper., Jacobson F, Guo H, Olesen K, Okvist M, Neutze R, Sjolin L, Acta Crystallogr D Biol Crystallogr. 2005 Sep;61(Pt 9):1190-8. Epub 2005, Aug 16. PMID:16131751

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