2D5I
The crystal structure of AzoR (Azo Reductase) from Escherichia coli
Summary for 2D5I
| Entry DOI | 10.2210/pdb2d5i/pdb |
| Descriptor | Azo Reductase, FLAVIN MONONUCLEOTIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | azo reductase, oxidoreductase |
| Biological source | Escherichia coli |
| Total number of polymer chains | 1 |
| Total formula weight | 22187.97 |
| Authors | Ito, K.,Tanokura, M. (deposition date: 2005-11-02, release date: 2006-05-16, Last modification date: 2024-03-13) |
| Primary citation | Ito, K.,Nakanishi, M.,Lee, W.C.,Sasaki, H.,Zenno, S.,Saigo, K.,Kitade, Y.,Tanokura, M. Three-dimensional structure of AzoR from Escherichia coli. An oxidereductase conserved in microorganisms J.Biol.Chem., 281:20567-20576, 2006 Cited by PubMed Abstract: 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. PubMed: 16684776DOI: 10.1074/jbc.M513345200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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