View source for 3wec


==Structure of P450 RauA (CYP1050A1) complexed with a biosynthetic intermediate of aurachin RE==
<StructureSection load='3wec' size='340' side='right'caption='[[3wec]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wec]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_erythropolis Rhodococcus erythropolis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WEC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WEC FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AUI:3-[(2E,6E,9R)-9-HYDROXY-3,7,11-TRIMETHYLDODECA-2,6,10-TRIEN-1-YL]-2-METHYLQUINOLIN-4(1H)-ONE'>AUI</scene>, <scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene></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=3wec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wec OCA], [https://pdbe.org/3wec PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wec RCSB], [https://www.ebi.ac.uk/pdbsum/3wec PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wec ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/S6BVH1_RHOER S6BVH1_RHOER] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cytochrome P450 RauA from Rhodococcus erythropolis JCM 6824 catalyzes the hydroxylation of a nitrogen atom in the quinolone ring of aurachin, thereby conferring strong antibiotic activity on the aurachin alkaloid. Here, we report the crystal structure of RauA in complex with its substrate, a biosynthetic intermediate of aurachin RE. Clear electron density showed that the quinolone ring is oriented parallel to the porphyrin plane of the heme cofactor, while the farnesyl chain curls into a U-shape topology and is buried inside the solvent-inaccessible hydrophobic interior of RauA. The nearest atom from the heme iron is the quinolone nitrogen (4.3A), which is consistent with RauA catalyzing the N-hydroxylation of the quinolone ring to produce mature aurachin RE.

Structure of the quinoline N-hydroxylating cytochrome P450 RauA, an essential enzyme that confers antibiotic activity on aurachin alkaloids.,Yasutake Y, Kitagawa W, Hata M, Nishioka T, Ozaki T, Nishiyama M, Kuzuyama T, Tamura T FEBS Lett. 2014 Jan 3;588(1):105-10. doi: 10.1016/j.febslet.2013.11.016. Epub, 2013 Nov 20. PMID:24269679<ref>PMID:24269679</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wec" style="background-color:#fffaf0;"></div>

==See Also==
*[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Rhodococcus erythropolis]]
[[Category: Kitagawa W]]
[[Category: Tamura T]]
[[Category: Yasutake Y]]