1gs8

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1gs8, resolution 1.90Å

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CRYSTAL STRUCTURE OF MUTANT D92N ALCALIGENES XYLOSOXIDANS NITRITE REDUCTASE

Overview

Dissimilatory nitrite reductase catalyses the reduction of nitrite, (NO(2)(-)) to nitric oxide (NO). Copper-containing nitrite reductases, contain both type 1 and type 2 Cu sites. Electron transfer from redox, partners is presumed to be mediated via the type 1 Cu site and used at the, catalytic type 2 Cu centre along with the substrate nitrite. At the type 2, Cu site, Asp92 has been identified as a key residue in substrate, utilisation, since it hydrogen bonds to the water molecule at the nitrite, binding site. We have also suggested that protons enter the catalytic site, via Asp92, through a water network that is mediated by His254. The role of, these residues has been investigated in the blue copper nitrite reductase, from Alcaligenes xylosoxidans (NCIMB 11015) by a combination of ... [(full description)]

About this Structure

1GS8 is a [Single protein] structure of sequence from [Achromobacter xylosoxidans] with CU and ZN as [ligands]. Active as [Transferred entry: 1.7.2.1], with EC number [1.7.99.3]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Biochemical and crystallographic studies of the Met144Ala, Asp92Asn and His254Phe mutants of the nitrite reductase from Alcaligenes xylosoxidans provide insight into the enzyme mechanism., Ellis MJ, Prudencio M, Dodd FE, Strange RW, Sawers G, Eady RR, Hasnain SS, J Mol Biol. 2002 Feb 8;316(1):51-64. PMID:11829502

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