5fbt: Difference between revisions
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<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 with sequence from [ | <table><tr><td colspan='2'>[[5fbt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_monocytogenes_serotype_4b_str._F2365 Listeria monocytogenes serotype 4b str. F2365]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5FBT FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.702Å</td></tr> | ||
<tr id=' | <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>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5fbt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5fbt OCA], [https://pdbe.org/5fbt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5fbt RCSB], [https://www.ebi.ac.uk/pdbsum/5fbt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5fbt ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A0X1KHF9_LISMF A0A0X1KHF9_LISMF] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Listeria monocytogenes serotype 4b str. F2365]] | ||
[[Category: Anderson | [[Category: Anderson WF]] | ||
[[Category: Savchenko A]] | |||
[[Category: Savchenko | [[Category: Skarina T]] | ||
[[Category: Skarina | [[Category: Stogios PJ]] | ||
[[Category: Stogios | [[Category: Wawrzak Z]] | ||
[[Category: Wawrzak | [[Category: Yim V]] | ||
[[Category: Yim | |||
Revision as of 09:45, 19 July 2023
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
FunctionPublication 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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