3chi: Difference between revisions

Revision as of 08:55, 16 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3chi.png

Template:STRUCTURE 3chi

Crystal Structure of Di-iron AurF (Monoclinic form)Crystal Structure of Di-iron AurF (Monoclinic form)

Template:ABSTRACT PUBMED 18458342

About this StructureAbout this Structure

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

ReferenceReference

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 08:55:37 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:3chi.jpg|left|200px]]
+{{Seed}}
+[[Image:3chi.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_3chi|  PDB=3chi  |  SCENE=  }}
-'''Crystal Structure of Di-iron AurF (Monoclinic form)'''
+===Crystal Structure of Di-iron AurF (Monoclinic form)===
-==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 09:21:59 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 16 08:55:37 2008''