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- | [[Image:3chh.jpg|left|200px]] | |
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- | <!--
| + | ==Crystal Structure of Di-iron AurF== |
- | The line below this paragraph, containing "STRUCTURE_3chh", creates the "Structure Box" on the page.
| + | <StructureSection load='3chh' size='340' side='right'caption='[[3chh]], [[Resolution|resolution]] 2.00Å' scene=''> |
- | You may change the PDB parameter (which sets the PDB file loaded into the applet)
| + | == Structural highlights == |
- | or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
| + | <table><tr><td colspan='2'>[[3chh]] 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=3CHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3CHH FirstGlance]. <br> |
- | or leave the SCENE parameter empty for the default display.
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</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> |
- | {{STRUCTURE_3chh| PDB=3chh | SCENE= }}
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3chh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3chh OCA], [https://pdbe.org/3chh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3chh RCSB], [https://www.ebi.ac.uk/pdbsum/3chh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3chh ProSAT]</span></td></tr> |
- | | + | </table> |
- | '''Crystal Structure of Di-iron AurF'''
| + | == 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:20798054, PubMed:18458342). 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 == |
- | ==Overview== | + | [[Image:Consurf_key_small.gif|200px|right]] |
- | 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.
| + | Check<jmol> |
- | | + | <jmolCheckbox> |
- | ==About this Structure== | + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ch/3chh_consurf.spt"</scriptWhenChecked> |
- | 3CHH is a [[Single protein]] structure of 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=3CHH OCA].
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
- | | + | <text>to colour the structure by Evolutionary Conservation</text> |
- | ==Reference== | + | </jmolCheckbox> |
- | 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:[http://www.ncbi.nlm.nih.gov/pubmed/18458342 18458342]
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3chh ConSurf]. |
- | [[Category: Single protein]] | + | <div style="clear:both"></div> |
| + | == References == |
| + | <references/> |
| + | __TOC__ |
| + | </StructureSection> |
| + | [[Category: Large Structures]] |
| [[Category: Streptomyces thioluteus]] | | [[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]]
| + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 28 09:21:57 2008''
| + | |
| Structural highlights
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:20798054, PubMed:18458342). 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.
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
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