3wec
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of P450 RauA (CYP1050A1) complexed with a biosynthetic intermediate of aurachin RE== | |
| + | <StructureSection load='3wec' size='340' side='right'caption='[[3wec]], [[Resolution|resolution]] 2.19Å' 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]] 2.19Å</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®/PubMed®, 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]] | ||
Current revision
Structure of P450 RauA (CYP1050A1) complexed with a biosynthetic intermediate of aurachin RE
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