Journal
CELL
Volume 122, Issue 4, Pages 541-552Publisher
CELL PRESS
DOI: 10.1016/j.cell.2005.07.017
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Funding
- Howard Hughes Medical Institute Funding Source: Medline
- NIAID NIH HHS [R37 AI027690-15, AI27690, R37 AI027690-16, R37 AI027690, R37 AI027690-14, R37 AI027690-13, R01 AI027690] Funding Source: Medline
- NIGMS NIH HHS [R37 GM041376, R01 GM041376, R01 GM041376-17, P01 GM066671-02, R01 GM021589, R01 GM041376-14, R01 GM054098, GM21589, R01 GM041376-16, P01 GM066671, GM66671, R01 GM041376-15, GM41376, R01 GM054098-05, GM54098] Funding Source: Medline
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We define the target, mechanism, and structural basis of inhibition of bacterial RNA polymerase (RNAP) by the tetramic acid antibiotic streptolydigin (Stl). Stl binds to a site adjacent to but not overlapping the RNAP active center and stabilizes an RNAP-active-center conformational state with a straight-bridge helix. The results provide direct support for the proposals that alternative straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations exist and that cycling between straight-bridge-helix and bent-bridge-helix RNAP-active-center conformations is required for RNAP function. The results set bounds on models for RNAP function and suggest strategies for design of novel antibacterial agents.
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