5FBU
Crystal structure of rifampin phosphotransferase RPH-Lm from Listeria monocytogenes in complex with rifampin-phosphate
Summary for 5FBU
| Entry DOI | 10.2210/pdb5fbu/pdb |
| Related | 5FBS 5FBT |
| Descriptor | Phosphoenolpyruvate synthase, Rifampin-phosphate, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | antibiotic resistance, rifamycins, rifampin, phosphotransferase, atp grasp domain, phosphohistidine domain, structural genomics, center for structural genomics of infectious diseases, csgid, transferase-antibiotic complex, transferase/antibiotic |
| Biological source | Listeria monocytogenes serotype 4b str. F2365 |
| Total number of polymer chains | 1 |
| Total formula weight | 98042.28 |
| Authors | Stogios, P.J.,Wawrzak, Z.,Skarina, T.,Yim, V.,Savchenko, A.,Anderson, W.F.,Center for Structural Genomics of Infectious Diseases (CSGID) (deposition date: 2015-12-14, release date: 2015-12-30, Last modification date: 2023-09-27) |
| Primary citation | Stogios, P.J.,Cox, G.,Spanogiannopoulos, P.,Pillon, M.C.,Waglechner, N.,Skarina, T.,Koteva, K.,Guarne, A.,Savchenko, A.,Wright, G.D. Rifampin phosphotransferase is an unusual antibiotic resistance kinase. Nat Commun, 7:11343-11343, 2016 Cited by PubMed Abstract: 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. PubMed: 27103605DOI: 10.1038/ncomms11343 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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