5fbu | pdb_00005fbu

Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin-phosphate

spinqualitylabelsall models 5fbu, resolution 2.85Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5fbu is a 1 chain structure with sequence from Listeria monocytogenes serotype 4b str. F2365. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.85Å Ligands: 5WP, CL, MPD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0X1KHF9_LISMF 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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