4c0x

The crystal strucuture of PpAzoR in complex with anthraquinone-2- sulfonate

spinqualitylabelsall models 4c0x, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4c0x is a 1 chain structure with sequence from "bacillus_fluorescens_putidus"_flugge_1886 "bacillus fluorescens putidus" flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: AQN, FMN, GOL, PG4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [AZOR1_PSEPK] Catalyzes the reductive cleavage of azo bond in aromatic azo compounds to the corresponding amines. Requires NADH, but not NADPH, as an electron donor for its activity (By similarity). Publication Abstract from PubMed Enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this paper we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 A), of PpAzoR in complex with the anthraquinone-2-sulfonate (1.50 A) and of PpAzoR in complex with Reactive Black 5 dye (1.90 A). These structures reveal the residues and subtle changes that accompany substrate binding and release. Such changes highlight the fine control of access to the catalytic site that is required by the ping-pong mechanism, and in turn the specificity offered by the enzyme towards different substrates. The topology surrounding the active site shows novel features of substrate recognition and binding that help to explain and differentiate the substrate specificity observed among different bacterial azoreductases. This article is protected by copyright. All rights reserved. The Crystal Structure of Pseudomonas putida AzoR: the active site revisited.,Goncalves AM, Mendes S, de Sanctis D, Martins LO, Bento I FEBS J. 2013 Oct 16. doi: 10.1111/febs.12568. PMID:24127652 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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