2d5i: Difference between revisions

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[[Image:2d5i.gif|left|200px]]
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{{STRUCTURE_2d5i|  PDB=2d5i  |  SCENE=  }}  
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'''The crystal structure of AzoR (Azo Reductase) from Escherichia coli'''
===The crystal structure of AzoR (Azo Reductase) from Escherichia coli===




==Overview==
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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.
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{{ABSTRACT_PUBMED_16684776}}


==About this Structure==
==About this Structure==
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[[Category: Azo reductase]]
[[Category: Azo reductase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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Revision as of 06:08, 28 July 2008

File:2d5i.png

Template:STRUCTURE 2d5i

The crystal structure of AzoR (Azo Reductase) from Escherichia coli

Template:ABSTRACT PUBMED 16684776

About this Structure

2D5I 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

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