1qni

From Proteopedia

Revision as of 14:57, 5 November 2007

CRYSTAL STRUCTURE OF NITROUS OXIDE REDUCTASE FROM PSEUDOMONAS NAUTICA, AT 2.4A RESOLUTION

Overview

Nitrous oxide (N20) is a greenhouse gas, the third most significant, contributor to global warming. As a key process for N20 elimination from, the biosphere, N20 reductases catalyze the two-electron reduction of N20, to N2. These 2 x 65 kDa copper enzymes are thought to contain a CuA, electron entry site, similar to that of cytochrome c oxidase, and a CuZ, catalytic center. The copper anomalous signal was used to solve the, crystal structure of N20 reductase from Pseudomonas nautica by, multiwavelength anomalous dispersion, to a resolution of 2.4 A. The, structure reveals that the CuZ center belongs to a new type of metal, cluster, in which four copper ions are liganded by seven histidine, residues. N20 binds to this center via a single copper ion. The remaining, copper ions might act as an electron reservoir, assuring a fast electron, transfer and avoiding the formation of dead-end products.

About this Structure

1QNI is a Single protein structure of sequence from Marinobacter hydrocarbonoclasticus with CA, CL, CUA and CUZ as ligands. Structure known Active Sites: CUA, CUB, CUC, CUD, CUE, CUF, CUU, CUV, CUW, CUX, CUY and CUZ. Full crystallographic information is available from OCA.

Reference

A novel type of catalytic copper cluster in nitrous oxide reductase., Brown K, Tegoni M, Prudencio M, Pereira AS, Besson S, Moura JJ, Moura I, Cambillau C, Nat Struct Biol. 2000 Mar;7(3):191-5. PMID:10700275

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