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Literature DB >> 16122422

Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation.

Steven Tuske¹, Stefan G Sarafianos, Xinyue Wang, Brian Hudson, Elena Sineva, Jayanta Mukhopadhyay, Jens J Birktoft, Olivier Leroy, Sajida Ismail, Arthur D Clark, Chhaya Dharia, Andrew Napoli, Oleg Laptenko, Jookyung Lee, Sergei Borukhov, Richard H Ebright, Eddy Arnold.

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-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.

Entities: Chemical

Mesh：

Substances：

Year: 2005 PMID： 16122422 PMCID： PMC2754413 DOI： 10.1016/j.cell.2005.07.017

Source DB: PubMed Journal: Cell ISSN： 0092-8674 Impact factor: 41.582

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