3chh: Difference between revisions

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[[Image:3chh.~~jpg~~|left|200px]]

[[Image:3chh.png|left|200px]]

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~~'''~~Crystal Structure of Di-iron AurF~~'''~~

===Crystal Structure of Di-iron AurF===

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_18458342}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 18458342 is the PubMed ID number.

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==About this Structure==

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[[Category: Di-iron oxygenase]]

[[Category: Oxidoreductase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~May 28 09~~:21:57 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:53:19 2008''

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-[[Image:3chh.jpg|left|200px]]
+{{Seed}}
+[[Image:3chh.png|left|200px]]
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 {{STRUCTURE_3chh|  PDB=3chh  |  SCENE=  }}
-'''Crystal Structure of Di-iron AurF'''
+===Crystal Structure of Di-iron AurF===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_18458342}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18458342 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_18458342}}
 ==About this Structure==
@@ Line 27: / Line 31: @@
 [[Category: Di-iron oxygenase]]
 [[Category: Oxidoreductase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:21:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:53:19 2008''