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Structures of RNA polymerase-antibiotic complexes Ho MX; Hudson BP; Das K; Arnold E; Ebright RHCurr Opin Struct Biol 2009[Dec]; 19 (6): 715-23Inhibition of bacterial RNA polymerase (RNAP) is an established strategy for antituberculosis therapy and broad-spectrum antibacterial therapy. Crystal structures of RNAP-inhibitor complexes are available for four classes of antibiotics: rifamycins, sorangicin, streptolydigin, and myxopyronin. The structures define three different targets, and three different mechanisms, for inhibition of bacterial RNAP: (1) rifamycins and sorangicin bind near the RNAP active center and block extension of RNA products; (2) streptolydigin interacts with a target that overlaps the RNAP active center and inhibits conformational cycling of the RNAP active center; and (3) myxopyronin interacts with a target remote from the RNAP active center and functions by interfering with opening of the RNAP active-center cleft to permit entry and unwinding of DNA and/or by interfering with interactions between RNAP and the DNA template strand. The structures enable construction of homology models of pathogen RNAP-antibiotic complexes, enable in silico screening for new antibacterial agents, and enable rational design of improved antibacterial agents.|Anti-Bacterial Agents/*chemistry/*metabolism/pharmacology[MESH]|Bacteria/drug effects/enzymology[MESH]|DNA-Directed RNA Polymerases/*chemistry/*metabolism[MESH]|Models, Molecular[MESH]|Protein Binding[MESH]|Sequence Homology, Amino Acid[MESH] |
