1ZYR
Structure of Thermus thermophilus RNA polymerase holoenzyme in complex with the antibiotic streptolydigin
Summary for 1ZYR
Entry DOI | 10.2210/pdb1zyr/pdb |
Related | 1I6H 1IW7 1K83 1SMY 1YNJ 1YNN |
Descriptor | DNA-directed RNA polymerase alpha chain, DNA-directed RNA polymerase beta chain, DNA-directed RNA polymerase subunit beta' chain, ... (8 entities in total) |
Functional Keywords | rna polymerase; streptolydigin; transcription; holoenzyme, transcription, transferase |
Biological source | Thermus thermophilus More |
Total number of polymer chains | 12 |
Total formula weight | 854782.62 |
Authors | Tuske, 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. (deposition date: 2005-06-10, release date: 2005-09-13, Last modification date: 2023-08-23) |
Primary citation | Tuske, 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: 16122422DOI: 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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