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3chh

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{{STRUCTURE_3chh| PDB=3chh | SCENE= }}
{{STRUCTURE_3chh| PDB=3chh | SCENE= }}
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'''Crystal Structure of Di-iron AurF'''
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===Crystal Structure of Di-iron AurF===
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==Overview==
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p-Aminobenzoate N-oxygenase (AurF) from Streptomyces thioluteus catalyzes the formation of unusual polyketide synthase starter unit p-nitrobenzoic acid (pNBA) from p-aminobenzoic acid (pABA) in the biosynthesis of antibiotic aureothin. AurF is a metalloenzyme, but its native enzymatic activity has not been demonstrated in vitro, and its catalytic mechanism is unclear. In addition, the nature of the cofactor remains a controversy. Here, we report the in vitro reconstitution of the AurF enzyme activity, the crystal structure of AurF in the oxidized state, and the cocrystal structure of AurF with its product pNBA. Our combined biochemical and structural analysis unequivocally indicates that AurF is a non-heme di-iron monooxygenase that catalyzes sequential oxidation of aminoarenes to nitroarenes via hydroxylamine and nitroso intermediates.
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{{ABSTRACT_PUBMED_18458342}}
==About this Structure==
==About this Structure==
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[[Category: Di-iron oxygenase]]
[[Category: Di-iron oxygenase]]
[[Category: Oxidoreductase]]
[[Category: Oxidoreductase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:53:19 2008''

Revision as of 05:53, 16 July 2008

Image:3chh.png

Template:STRUCTURE 3chh

Crystal Structure of Di-iron AurF

Template:ABSTRACT PUBMED 18458342

About this Structure

3CHH is a Single protein structure of sequence from Streptomyces thioluteus. Full crystallographic information is available from OCA.

Reference

In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis., Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H, Proc Natl Acad Sci U S A. 2008 May 13;105(19):6858-63. Epub 2008 May 5. PMID:18458342

Page seeded by OCA on Wed Jul 16 08:53:19 2008

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