2CW0
Crystal structure of Thermus thermophilus RNA polymerase holoenzyme at 3.3 angstroms resolution
Summary for 2CW0
Entry DOI | 10.2210/pdb2cw0/pdb |
Descriptor | DNA-directed RNA polymerase alpha chain, DNA-directed RNA polymerase beta chain, DNA-directed RNA polymerase beta' chain, ... (7 entities in total) |
Functional Keywords | rna polymerase holoenzyme, transcription, bent-bridge helix, transferase |
Biological source | Thermus thermophilus More |
Total number of polymer chains | 12 |
Total formula weight | 853581.22 |
Authors | Tuske, S.,Sarafianos, S.G.,Wang, X.,Hudson, B.,Sineva, E.,Mukhopadhyay, J.,Birktoft, J.J.,Leroy, O.,Ismail, S.,Clark Jr., A.D.,Dharia, C.,Napoli, A.,Laptenko, O.,Lee, J.,Borukhov, S.,Ebright, R.H.,Arnold, E. (deposition date: 2005-06-15, release date: 2005-09-20, Last modification date: 2023-10-25) |
Primary citation | Tuske, S.,Sarafianos, S.G.,Wang, X.,Hudson, B.,Sineva, E.,Mukhopadhyay, J.,Birktoft, J.J.,Leroy, O.,Ismail, S.,Clark Jr., 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 (3.3 Å) |
Structure validation
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