5fbt: Difference between revisions
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==Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin== | ==Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin== | ||
<StructureSection load='5fbt' size='340' side='right' caption='[[5fbt]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='5fbt' size='340' side='right'caption='[[5fbt]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5fbt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FBT OCA]. For a <b>guided tour on the structure components</b> use [http:// | <table><tr><td colspan='2'>[[5fbt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lismf Lismf]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FBT OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5FBT FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5WQ:RIFAMPIN'>5WQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5WQ:RIFAMPIN'>5WQ</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fbs|5fbs]], [[5fbu|5fbu]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5fbs|5fbs]], [[5fbu|5fbu]]</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LmNIHS28_01948 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=265669 LISMF])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5fbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fbt OCA], [http://pdbe.org/5fbt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5fbt RCSB], [http://www.ebi.ac.uk/pdbsum/5fbt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5fbt ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Lismf]] | |||
[[Category: Anderson, W F]] | [[Category: Anderson, W F]] | ||
[[Category: Structural genomic]] | [[Category: Structural genomic]] | ||
Revision as of 11:09, 29 April 2020
Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampinCrystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin
Structural highlights
Publication Abstract from PubMedRifampin (RIF) phosphotransferase (RPH) confers antibiotic resistance by conversion of RIF and ATP, to inactive phospho-RIF, AMP and Pi. Here we present the crystal structure of RPH from Listeria monocytogenes (RPH-Lm), which reveals that the enzyme is comprised of three domains: two substrate-binding domains (ATP-grasp and RIF-binding domains); and a smaller phosphate-carrying His swivel domain. Using solution small-angle X-ray scattering and mutagenesis, we reveal a mechanism where the swivel domain transits between the spatially distinct substrate-binding sites during catalysis. RPHs are previously uncharacterized dikinases that are widespread in environmental and pathogenic bacteria. These enzymes are members of a large unexplored group of bacterial enzymes with substrate affinities that have yet to be fully explored. Such an enzymatically complex mechanism of antibiotic resistance augments the spectrum of strategies used by bacteria to evade antimicrobial compounds. Rifampin phosphotransferase is an unusual antibiotic resistance kinase.,Stogios PJ, Cox G, Spanogiannopoulos P, Pillon MC, Waglechner N, Skarina T, Koteva K, Guarne A, Savchenko A, Wright GD Nat Commun. 2016 Apr 22;7:11343. doi: 10.1038/ncomms11343. PMID:27103605[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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