4C14

The crystal strucuture of PpAzoR in complex with reactive black 5 (RB5)

Summary for 4C14

• Entry DOI: 10.2210/pdb4c14/pdb
• Related: 4C0W
• Descriptor: FMN-DEPENDENT NADH-AZOREDUCTASE 1, [5-[3-[2-[[4-[2-[1-azanyl-7-[2-[4-[methyl-bis(oxidanyl)-$l^{4}-sulfanyl]phenyl]hydrazinyl]-8-oxidanyl-3,6-bis[tris(oxidanyl)-$l^{4}-sulfanyl]naphthalen-2-yl]hydrazinyl]phenyl]-bis(oxidanyl)-$l^{4}-sulfanyl]ethoxy]-7,8-dimethyl-2,4-bis(oxidanylidene)benzo[g]pteridin-10-yl]-2,3,4-tris(oxidanyl)pentyl] dihydrogen phosphate, DODECAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: oxidoreductase
• Biological source: PSEUDOMONAS PUTIDA
• Total number of polymer chains: 1
• Total formula weight: 23112.91

Authors

Goncalves, A.M.D.,de Sanctis, D.,Bento, I. (deposition date: 2013-08-09, release date: 2013-10-30, Last modification date: 2023-12-20)

Primary citation

Goncalves, A.M.,Mendes, S.,de Sanctis, D.,Martins, L.O.,Bento, I.
The crystal structure of Pseudomonas putida azoreductase - the active site revisited.
FEBS J., 280:6643-6657, 2013

PubMed Abstract: The enzymatic degradation of azo dyes begins with the reduction of the azo bond. In this article, we report the crystal structures of the native azoreductase from Pseudomonas putida MET94 (PpAzoR) (1.60 Å), of PpAzoR in complex with anthraquinone-2-sulfonate (1.50 Å), and of PpAzoR in complex with Reactive Black 5 dye (1.90 Å). 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.

PubMed: 24127652
DOI: 10.1111/febs.12568

Experimental method

X-RAY DIFFRACTION (1.9 Å)