6brd

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<table><tr><td colspan='2'>[[6brd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strvp Strvp]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5vqc 5vqc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BRD FirstGlance]. <br>
<table><tr><td colspan='2'>[[6brd]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Strvp Strvp]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5vqc 5vqc]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BRD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BRD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RFP:RIFAMPICIN'>RFP</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=RFP:RIFAMPICIN'>RFP</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5vqb|5vqb]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SVEN_0481 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=953739 STRVP])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SVEN_0481 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=953739 STRVP])</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=6brd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6brd OCA], [http://pdbe.org/6brd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6brd RCSB], [http://www.ebi.ac.uk/pdbsum/6brd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6brd ProSAT]</span></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=6brd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6brd OCA], [http://pdbe.org/6brd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6brd RCSB], [http://www.ebi.ac.uk/pdbsum/6brd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6brd ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rifamycin monooxygenases (Rox) are present in a variety of environmental bacteria and are associated with decomposition of the clinically utilized antibiotic rifampin. Here we report the structure and function of a drug-inducible rox gene from Streptomyces venezuelae, which encodes a class A flavoprotein monooxygenase that inactivates a broad range of rifamycin antibiotics. Our findings describe a mechanism of rifamycin inactivation initiated by monooxygenation of the 2-position of the naphthyl group, which subsequently results in ring opening and linearization of the antibiotic. The result is an antibiotic that no longer adopts the basket-like structure essential for binding to the RNA exit tunnel of the target RpoB, thereby providing the molecular logic of resistance. This unique mechanism of enzymatic inactivation underpins the broad spectrum of rifamycin resistance mediated by Rox enzymes and presents a new antibiotic resistance mechanism not yet seen in microbial antibiotic detoxification.
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Rox, a Rifamycin Resistance Enzyme with an Unprecedented Mechanism of Action.,Koteva K, Cox G, Kelso JK, Surette MD, Zubyk HL, Ejim L, Stogios P, Savchenko A, Sorensen D, Wright GD Cell Chem Biol. 2018 Jan 26. pii: S2451-9456(18)30031-X. doi:, 10.1016/j.chembiol.2018.01.009. PMID:29398560<ref>PMID:29398560</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6brd" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 08:28, 22 February 2018

Crystal structure of rifampin monooxygenase from Streptomyces venezuelae, complexed with rifampin and FAD

6brd, resolution 3.32Å

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