1v4b: Difference between revisions
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'''The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form''' | '''The crystal structure of AzoR (Azo Reductase) from Escherichia coli: Oxidized form''' | ||
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[[Category: Ito, K.]] | [[Category: Ito, K.]] | ||
[[Category: Tanokura, M.]] | [[Category: Tanokura, M.]] | ||
[[Category: | [[Category: Azo reductase]] | ||
[[Category: | [[Category: Oxidoreductase]] | ||
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Revision as of 09:03, 3 May 2008
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. 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 Sat May 3 12:03:42 2008
