1zyr

File:1zyr.gif

spinqualitylabelsall models 1zyr, resolution 3.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin

OverviewOverview

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.

About this StructureAbout this Structure

1ZYR is a Protein complex structure of sequences from Thermus thermophilus with STD, ZN and MG as ligands. Active as DNA-directed RNA polymerase, with EC number 2.7.7.6 Full crystallographic information is available from OCA.

ReferenceReference

Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation., Tuske S, Sarafianos SG, Wang X, Hudson B, Sineva E, Mukhopadhyay J, Birktoft JJ, Leroy O, Ismail S, Clark AD Jr, Dharia C, Napoli A, Laptenko O, Lee J, Borukhov S, Ebright RH, Arnold E, Cell. 2005 Aug 26;122(4):541-52. PMID:16122422

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