Author/Authors :
Tuske، Steven نويسنده , , Sarafianos، Stefan G. نويسنده , , Wang، Xinyue نويسنده , , Hudson، Brian نويسنده , , Sineva، Elena نويسنده , , Mukhopadhyay، Jayanta نويسنده , , Birktoft، Jens J. نويسنده , , Leroy، Olivier نويسنده , , Ismail، Sajida نويسنده , , Clark، Arthur D. نويسنده , , Dharia، Chhaya نويسنده , , Napoli، Andrew نويسنده , , Laptenko، Oleg نويسنده , , Lee، Jookyung نويسنده , , Borukhov، Sergei نويسنده , , Ebright، Richard H. نويسنده , , Arnold، Eddy نويسنده ,
Abstract :
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-bridgehelix 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.
Keywords :
DIGLYPHUS ISAEA , Liriomyza trifolii , Abamectin compatibility , IPM , Biological control , Greenhouse
