3chu: Difference between revisions

Latest revision as of 09:01, 13 August 2026

Crystal Structure of Di-iron Aurf

Structural highlights

3chu is a 2 chain structure with sequence from Streptomyces thioluteus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.2Å
Ligands:	FEO
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AURF_STRTU Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:18458342, PubMed:20798054). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).^[1] ^[2] ^[3] ^[4] ^[5] ^[6]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[7]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ He J, Hertweck C. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem Biol. 2003 Dec;10(12):1225-32. PMID:14700630 doi:10.1016/j.chembiol.2003.11.009
↑ He J, Hertweck C. Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: involvement of an unprecedented N-oxygenase. J Am Chem Soc. 2004 Mar 31;126(12):3694-5. PMID:15038705 doi:10.1021/ja039328t
↑ Simurdiak M, Lee J, Zhao H. A new class of arylamine oxygenases: evidence that p-aminobenzoate N-oxygenase (AurF) is a di-iron enzyme and further mechanistic studies. Chembiochem. 2006 Aug;7(8):1169-72. PMID:16927313 doi:10.1002/cbic.200600136
↑ Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H. In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis. Proc Natl Acad Sci U S A. 2008 May 13;105(19):6858-63. Epub 2008 May 5. PMID:18458342
↑ Korboukh VK, Li N, Barr EW, Bollinger JM Jr, Krebs C. A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. J Am Chem Soc. 2009 Sep 30;131(38):13608-9. PMID:19731912 doi:10.1021/ja9064969
↑ Li N, Korboukh VK, Krebs C, Bollinger JM Jr. Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus. Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15722-7. PMID:20798054 doi:10.1073/pnas.1002785107
↑ Choi YS, Zhang H, Brunzelle JS, Nair SK, Zhao H. In vitro reconstitution and crystal structure of p-aminobenzoate N-oxygenase (AurF) involved in aureothin biosynthesis. Proc Natl Acad Sci U S A. 2008 May 13;105(19):6858-63. Epub 2008 May 5. PMID:18458342

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] He J, Hertweck C. Iteration as programmed event during polyketide assembly; molecular analysis of the aureothin biosynthesis gene cluster. Chem Biol. 2003 Dec;10(12):1225-32. PMID:14700630 doi:10.1016/j.chembiol.2003.11.009

[2] He J, Hertweck C. Biosynthetic origin of the rare nitroaryl moiety of the polyketide antibiotic aureothin: involvement of an unprecedented N-oxygenase. J Am Chem Soc. 2004 Mar 31;126(12):3694-5. PMID:15038705 doi:10.1021/ja039328t

[3] Simurdiak M, Lee J, Zhao H. A new class of arylamine oxygenases: evidence that p-aminobenzoate N-oxygenase (AurF) is a di-iron enzyme and further mechanistic studies. Chembiochem. 2006 Aug;7(8):1169-72. PMID:16927313 doi:10.1002/cbic.200600136

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

[5] Korboukh VK, Li N, Barr EW, Bollinger JM Jr, Krebs C. A long-lived, substrate-hydroxylating peroxodiiron(III/III) intermediate in the amine oxygenase, AurF, from Streptomyces thioluteus. J Am Chem Soc. 2009 Sep 30;131(38):13608-9. PMID:19731912 doi:10.1021/ja9064969

[6] Li N, Korboukh VK, Krebs C, Bollinger JM Jr. Four-electron oxidation of p-hydroxylaminobenzoate to p-nitrobenzoate by a peroxodiferric complex in AurF from Streptomyces thioluteus. Proc Natl Acad Sci U S A. 2010 Sep 7;107(36):15722-7. PMID:20798054 doi:10.1073/pnas.1002785107

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

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[2]

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@@ Line 1: / Line 1: @@
 ==Crystal Structure of Di-iron Aurf==
-<StructureSection load='3chu' size='340' side='right' caption='[[3chu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+<StructureSection load='3chu' size='340' side='right'caption='[[3chu]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3chu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Streptomyces_thioluteus Streptomyces thioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CHU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3chu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_thioluteus Streptomyces thioluteus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3CHU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHU FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3chi|3chi]], [[3cht|3cht]], [[3chh|3chh]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FEO:MU-OXO-DIIRON'>FEO</scene></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aurF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66431 Streptomyces thioluteus])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3chu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chu OCA], [https://pdbe.org/3chu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chu RCSB], [https://www.ebi.ac.uk/pdbsum/3chu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chu ProSAT]</span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3chu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chu OCA], [http://pdbe.org/3chu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3chu RCSB], [http://www.ebi.ac.uk/pdbsum/3chu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3chu ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/AURF_STRTU AURF_STRTU] Involved in the biosynthesis of the polyketide antibiotic aureothin (PubMed:14700630, PubMed:15038705). Catalyzes the oxidation of p-aminobenzoate (pABA) to p-nitrobenzoate (pNBA), an unusual polyketide synthase starter unit (PubMed:15038705, PubMed:16927313, PubMed:18458342, PubMed:20798054). Reaction mechanism involves the generation of a peroxodiiron(III/III) intermediate, which effects the initial oxidation of p-aminobenzoate to p-hydroxylaminobenzoate (Ar-NHOH) (PubMed:19731912, PubMed:20798054). Ar-NHOH is then probably directly converted to the fully oxidized p-nitrobenzoate via a four-electron N-oxidation, bypassing the formation of a nitroso compound (PubMed:20798054).<ref>PMID:14700630</ref> <ref>PMID:15038705</ref> <ref>PMID:16927313</ref> <ref>PMID:18458342</ref> <ref>PMID:19731912</ref> <ref>PMID:20798054</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 14: / Line 15: @@
    <jmolCheckbox>
      <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chu_consurf.spt"</scriptWhenChecked>
-     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
      <text>to colour the structure by Evolutionary Conservation</text>
    </jmolCheckbox>
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Streptomyces thioluteus]]
-[[Category: Brunzelle, J S]]
+[[Category: Brunzelle JS]]
-[[Category: Nair, S K]]
+[[Category: Nair SK]]
-[[Category: Zhang, H]]
+[[Category: Zhang H]]
-[[Category: Di-iron oxygenase]]
-[[Category: Oxidoreductase]]

3chu: Difference between revisions

Latest revision as of 09:01, 13 August 2026

Crystal Structure of Di-iron Aurf

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

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