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1ZYR

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

Summary for 1ZYR
Entry DOI10.2210/pdb1zyr/pdb
Related1I6H 1IW7 1K83 1SMY 1YNJ 1YNN
DescriptorDNA-directed RNA polymerase alpha chain, DNA-directed RNA polymerase beta chain, DNA-directed RNA polymerase subunit beta' chain, ... (8 entities in total)
Functional Keywordsrna polymerase; streptolydigin; transcription; holoenzyme, transcription, transferase
Biological sourceThermus thermophilus
More
Total number of polymer chains12
Total formula weight854782.62
Authors
Primary citationTuske, S.,Sarafianos, S.G.,Wang, X.,Hudson, B.,Sineva, E.,Mukhopadhyay, J.,Birktoft, J.J.,Leroy, O.,Ismail, S.,Clark, A.D.,Dharia, C.,Napoli, A.,Laptenko, O.,Lee, J.,Borukhov, S.,Ebright, R.H.,Arnold, E.
Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation.
Cell(Cambridge,Mass.), 122:541-552, 2005
Cited by
PubMed 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.
PubMed: 16122422
DOI: 10.1016/j.cell.2005.07.017
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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