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5ysw
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal Structure Analysis of Rif16 in complex with R-L== | |
| + | <StructureSection load='5ysw' size='340' side='right' caption='[[5ysw]], [[Resolution|resolution]] 2.60Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ysw]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YSW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YSW FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=9LF:(2S,12E,14E,16S,17S,18R,19R,20R,21S,22R,23S,24E)-21-(acetyloxy)-5,6,17,19-tetrahydroxy-23-methoxy-2,4,12,16,18,20,22-heptamethyl-1,11-dioxo-1,2-dihydro-2,7-(epoxypentadeca[1,11,13]trienoimino)naphtho[2,1-b]furan-9-yl+hydroxyacetate'>9LF</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5ysw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ysw OCA], [http://pdbe.org/5ysw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ysw RCSB], [http://www.ebi.ac.uk/pdbsum/5ysw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ysw ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Rifamycin-derived drugs, including rifampin, rifabutin, rifapentine, and rifaximin, have long been used as first-line therapies for the treatment of tuberculosis and other deadly infections. However, the late steps leading to the biosynthesis of the industrially important rifamycin SV and B remain largely unknown. Here, we characterize a network of reactions underlying the biosynthesis of rifamycin SV, S, L, O, and B. The two-subunit transketolase Rif15 and the cytochrome P450 enzyme Rif16 are found to mediate, respectively, a unique C-O bond formation in rifamycin L and an atypical P450 ester-to-ether transformation from rifamycin L to B. Both reactions showcase interesting chemistries for these two widespread and well-studied enzyme families. | ||
| - | + | Deciphering the late steps of rifamycin biosynthesis.,Qi F, Lei C, Li F, Zhang X, Wang J, Zhang W, Fan Z, Li W, Tang GL, Xiao Y, Zhao G, Li S Nat Commun. 2018 Jun 14;9(1):2342. doi: 10.1038/s41467-018-04772-x. PMID:29904078<ref>PMID:29904078</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 5ysw" style="background-color:#fffaf0;"></div> |
| - | [[Category: Li, S | + | == References == |
| - | [[Category: Qi, F | + | <references/> |
| - | [[Category: Xiao, Y | + | __TOC__ |
| - | [[Category: | + | </StructureSection> |
| + | [[Category: Li, F W]] | ||
| + | [[Category: Li, S Y]] | ||
| + | [[Category: Qi, F F]] | ||
| + | [[Category: Xiao, Y L]] | ||
| + | [[Category: Zhao, G P]] | ||
| + | [[Category: Cytochrome p450]] | ||
| + | [[Category: Metal binding protein]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Rifamycin]] | ||
Revision as of 07:09, 4 July 2018
Crystal Structure Analysis of Rif16 in complex with R-L
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