Summary for 6EYD
| Entry DOI | 10.2210/pdb6eyd/pdb |
| EMDB information | 3983 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total) |
| Functional Keywords | transcription sigma, transcription |
| Biological source | Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) More |
| Total number of polymer chains | 6 |
| Total formula weight | 416403.15 |
| Authors | Kouba, T.,Barvik, I.,Krasny, L. (deposition date: 2017-11-11, release date: 2018-12-12, Last modification date: 2024-05-15) |
| Primary citation | Kouba, T.,Pospisil, J.,Hnilicova, J.,Sanderova, H.,Barvik, I.,Krasny, L. The Core and Holoenzyme Forms of RNA Polymerase fromMycobacterium smegmatis. J. Bacteriol., 201:-, 2019 Cited by PubMed Abstract: Bacterial RNA polymerase (RNAP) is essential for gene expression and as such is a valid drug target. Hence, it is imperative to know its structure and dynamics. Here, we present two as-yet-unreported forms of RNAP: core and holoenzyme containing σ but no other factors. Each form was detected by cryo-electron microscopy in two major conformations. Comparisons of these structures with known structures of other RNAPs reveal a high degree of conformational flexibility of the mycobacterial enzyme and confirm that region 1.1 of σ is directed into the primary channel of RNAP. Taken together, we describe the conformational changes of unrestrained mycobacterial RNAP. We describe here three-dimensional structures of core and holoenzyme forms of mycobacterial RNA polymerase (RNAP) solved by cryo-electron microscopy. These structures fill the thus-far-empty spots in the gallery of the pivotal forms of mycobacterial RNAP and illuminate the extent of conformational dynamics of this enzyme. The presented findings may facilitate future designs of antimycobacterial drugs targeting RNAP. PubMed: 30478083DOI: 10.1128/JB.00583-18 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.22 Å) |
Structure validation
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