Proceedings of the Japan Academy, Series B
Online ISSN : 1349-2896
Print ISSN : 0386-2208
ISSN-L : 0386-2208
Original Papers
Crystal structure of azoreductase AzoR from Escherichia coli
Kosuke ITOMasayuki NAKANISHIWoo Cheol LEEHiroshi SASAKIShuhei ZENNOKaoru SAIGOYukio KITADEMasaru TANOKURA
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2005 Volume 81 Issue 6 Pages 225-228

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Abstract

Azoreductase AzoR is an oxidoreductase isolated from Escherichia coli as an enzyme responsible for the reduction of azo compounds. As the first step toward the elucidation of the molecular mechanism of function, we determined the three-dimensional structure of the enzyme by X-ray crystallography at 1.8 Å resolution. The crystal structure has revealed that AzoR is an FMN-containing and homodimeric enzyme. Each monomer consists of a twisted central parallel β-sheet surrounded on both sides by helices. The overall folding of the protein resembles NQO1, originally called DT-diaphorase [NAD(P)H: quinone reductase, EC 1.6.99.2], a mammalian FAD containing protein without significant sequence identity.


(Communicated by Masanori OTSUKA, M.J.A.)

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© 2005 The Japan Academy
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