3wec
From Proteopedia
(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]] | ||
Revision as of 17:42, 21 December 2014
Structure of P450 RauA (CYP1050A1) complexed with a biosynthetic intermediate of aurachin RE
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