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<StructureSection load='3p3l' size='340' side='right'caption='[[3p3l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='3p3l' size='340' side='right'caption='[[3p3l]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3p3l]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/"streptomyces_thioluteus"_okami_1952 "streptomyces thioluteus" okami 1952]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3P3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P3L FirstGlance]. <br>
<table><tr><td colspan='2'>[[3p3l]] 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=3P3L OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3P3L FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3p3o|3p3o]], [[3p3x|3p3x]], [[3p3z|3p3z]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aurH ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=66431 "Streptomyces thioluteus" Okami 1952])</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=3p3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p3l OCA], [https://pdbe.org/3p3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p3l RCSB], [https://www.ebi.ac.uk/pdbsum/3p3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p3l ProSAT]</span></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=3p3l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p3l OCA], [https://pdbe.org/3p3l PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p3l RCSB], [https://www.ebi.ac.uk/pdbsum/3p3l PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p3l ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q70KH6_STRTU Q70KH6_STRTU]
AurH is a unique cytochrome P450 monooxygenase catalyzing the stepwise formation of a homochiral oxygen heterocycle, a key structural and pharmacophoric component of the antibiotic aureothin. The exceptional enzymatic reaction involves a tandem oxygenation process including a regio- and stereospecific hydroxylation, followed by heterocyclization. For the structural and biochemical basis of this unparalleled sequence, four crystal structures of AurH variants in different conformational states and in complex with the P450 inhibitor ancymidol were solved, which represent the first structures of the CYP151A group. Structural data in conjunction with computational docking, site-directed mutagenesis, and chemical analyses unveiled a switch function when recognizing the two substrates, deoxyaureothin and the hydroxylated intermediate, thus allowing the second oxygenation-heterocyclization step. Furthermore, we were able to modify the chemo- and regioselectivity of AurH, yielding mutants that catalyze the regioselective six-electron transfer of a nonactivated methyl group to a carboxylic acid via hydroxyl and aldehyde intermediates.
 
Structural Fine-Tuning of a Multifunctional Cytochrome P450 Monooxygenase.,Zocher G, Richter ME, Mueller U, Hertweck C J Am Chem Soc. 2011 Jan 31. PMID:21280577<ref>PMID:21280577</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3p3l" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Streptomyces thioluteus okami 1952]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Hertweck, C]]
[[Category: Streptomyces thioluteus]]
[[Category: Mueller, U]]
[[Category: Hertweck C]]
[[Category: Richter, M E.A]]
[[Category: Mueller U]]
[[Category: Zocher, G]]
[[Category: Richter MEA]]
[[Category: Cytochrome p450]]
[[Category: Zocher G]]
[[Category: Monooxygenase]]
[[Category: Oxidoreductase]]
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