5hv3: Difference between revisions
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<StructureSection load='5hv3' size='340' side='right' caption='[[5hv3]], [[Resolution|resolution]] 3.12Å' scene=''> | <StructureSection load='5hv3' size='340' side='right' caption='[[5hv3]], [[Resolution|resolution]] 3.12Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5hv3]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HV3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[5hv3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_monocytogenes_hominis"_nyfeldt_1932 "bacterium monocytogenes hominis" nyfeldt 1932]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5HV3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5HV3 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hv1|5hv1]], [[5hv2|5hv2]], [[5hv6|5hv6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hv1|5hv1]], [[5hv2|5hv2]], [[5hv6|5hv6]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ATE46_07415 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1639 "Bacterium monocytogenes hominis" Nyfeldt 1932])</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=5hv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hv3 OCA], [http://pdbe.org/5hv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5hv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hv3 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=5hv3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5hv3 OCA], [http://pdbe.org/5hv3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5hv3 RCSB], [http://www.ebi.ac.uk/pdbsum/5hv3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5hv3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacterium monocytogenes hominis nyfeldt 1932]] | |||
[[Category: Qi, X]] | [[Category: Qi, X]] | ||
[[Category: Zhang, P]] | [[Category: Zhang, P]] | ||
Revision as of 15:49, 6 November 2017
Rifampin phosphotransferase G527Y mutant in complex with AMPPNP from Listeria monocytogenesRifampin phosphotransferase G527Y mutant in complex with AMPPNP from Listeria monocytogenes
Structural highlights
Publication Abstract from PubMedRifampin (RIF) is a first-line drug used for the treatment of tuberculosis and other bacterial infections. Various RIF resistance mechanisms have been reported, and recently an RIF-inactivation enzyme, RIF phosphotransferase (RPH), was reported to phosphorylate RIF at its C21 hydroxyl at the cost of ATP. However, the underlying molecular mechanism remained unknown. Here, we solve the structures of RPH fromListeria monocytogenes(LmRPH) in different conformations. LmRPH comprises three domains: an ATP-binding domain (AD), an RIF-binding domain (RD), and a catalytic His-containing domain (HD). Structural analyses reveal that the C-terminal HD can swing between the AD and RD, like a toggle switch, to transfer phosphate. In addition to its catalytic role, the HD can bind to the AD and induce conformational changes that stabilize ATP binding, and the binding of the HD to the RD is required for the formation of the RIF-binding pocket. A line of hydrophobic residues forms the RIF-binding pocket and interacts with the 1-amino, 2-naphthol, 4-sulfonic acid and naphthol moieties of RIF. The R group of RIF points toward the outside of the pocket, explaining the low substrate selectivity of RPH. Four residues near the C21 hydroxyl of RIF, His825, Arg666, Lys670, and Gln337, were found to play essential roles in the phosphorylation of RIF; among these the His825 residue may function as the phosphate acceptor and donor. Our study reveals the molecular mechanism of RIF phosphorylation catalyzed by RPH and will guide the development of a new generation of rifamycins. Structural basis of rifampin inactivation by rifampin phosphotransferase.,Qi X, Lin W, Ma M, Wang C, He Y, He N, Gao J, Zhou H, Xiao Y, Wang Y, Zhang P Proc Natl Acad Sci U S A. 2016 Mar 21. pii: 201523614. PMID:27001859[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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