5ysm: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Crystal Structure Analysis of Rif16== | |||
<StructureSection load='5ysm' size='340' side='right' caption='[[5ysm]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ysm]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YSM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YSM FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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=5ysm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ysm OCA], [http://pdbe.org/5ysm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ysm RCSB], [http://www.ebi.ac.uk/pdbsum/5ysm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ysm 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> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5ysm" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Xiao, Y | <references/> | ||
[[Category: | __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 10:09, 4 July 2018
Crystal Structure Analysis of Rif16Crystal Structure Analysis of Rif16
Structural highlights
Publication Abstract from PubMedRifamycin-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||