1v4b
From Proteopedia
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The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form
Overview
The crystal structure of AzoR (azoreductase) has been determined in complex with FMN for two different crystal forms at 1.8 and 2.2 A resolution. AzoR is an oxidoreductase isolated from Escherichia coli as a protein responsible for the degradation of azo compounds. This enzyme is an FMN-dependent NADH-azoreductase and catalyzes the reductive cleavage of azo groups by a ping-pong mechanism. The structure suggests that AzoR acts in a homodimeric state forming the two identical catalytic sites to which both monomers contribute. The structure revealed that each monomer of AzoR has a flavodoxin-like structure, without the explicit overall amino acid sequence homology. Superposition of the structures from the two different crystal forms revealed the conformational change and suggested a mechanism for accommodating substrates of different size. Furthermore, comparison of the active site structure with that of NQO1 complexed with substrates provides clues to the possible substrate-binding mechanism of AzoR.
About this Structure
1V4B is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Azobenzene reductase, with EC number 1.7.1.6 Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms., Ito K, Nakanishi M, Lee WC, Sasaki H, Zenno S, Saigo K, Kitade Y, Tanokura M, J Biol Chem. 2006 Jul 21;281(29):20567-76. Epub 2006 May 9. PMID:16684776
Page seeded by OCA on Thu Feb 21 15:31:23 2008
Categories: Azobenzene reductase | Escherichia coli | Single protein | Ito, K. | Tanokura, M. | EDO | FMN | IPA | Azo reductase | Oxidoreductase
