3wec: Difference between revisions
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==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 [http://en.wikipedia.org/wiki/"mycobacterium_erythropolis"_gray_and_thornton_1928 "mycobacterium erythropolis" gray and thornton 1928]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WEC FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">rauA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1833 "Mycobacterium erythropolis" Gray and Thornton 1928])</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=3wec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wec OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3wec RCSB], [http://www.ebi.ac.uk/pdbsum/3wec PDBsum]</span></td></tr> | |||
</table> | |||
<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> | |||
[[Category: Kitagawa, W | |||
[[Category: Tamura, T | ==See Also== | ||
[[Category: Yasutake, Y | *[[Cytochrome P450|Cytochrome P450]] | ||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Mycobacterium erythropolis gray and thornton 1928]] | |||
[[Category: Kitagawa, W]] | |||
[[Category: Tamura, T]] | |||
[[Category: Yasutake, Y]] | |||
[[Category: Cytosolic enzyme]] | [[Category: Cytosolic enzyme]] | ||
[[Category: Heme]] | [[Category: Heme]] | ||
[[Category: Oxidoreductase]] | [[Category: Oxidoreductase]] | ||
[[Category: P450 fold]] | [[Category: P450 fold]] | ||
