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=''> | ||
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<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=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]</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=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]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rifampin (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<ref>PMID:27103605</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5fbt" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
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[[Category: Skarina, T]] | [[Category: Skarina, T]] | ||
[[Category: Stogios, P J]] | [[Category: Stogios, P J]] | ||
[[Category: Wawrzak, Z]] | |||
[[Category: Yim, V]] | [[Category: Yim, V]] | ||
[[Category: Antibiotic resistance]] | [[Category: Antibiotic resistance]] | ||
Revision as of 21:02, 10 May 2016
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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