8DKC
P. gingivalis RNA Polymerase
Summary for 8DKC
| Entry DOI | 10.2210/pdb8dkc/pdb |
| EMDB information | 27487 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (4 entities in total) |
| Functional Keywords | porphyromonas gingivalis, rna polymerase, transcription, cfb group bacteria |
| Biological source | Porphyromonas gingivalis More |
| Total number of polymer chains | 5 |
| Total formula weight | 390445.01 |
| Authors | |
| Primary citation | Bu, F.,Wang, X.,Li, M.,Ma, L.,Wang, C.,Hu, Y.,Cao, Z.,Liu, B. Cryo-EM Structure of Porphyromonas gingivalis RNA Polymerase. J.Mol.Biol., 436:168568-168568, 2024 Cited by PubMed Abstract: Porphyromonas gingivalis, an anaerobic CFB (Cytophaga, Fusobacterium, and Bacteroides) group bacterium, is the keystone pathogen of periodontitis and has been implicated in various systemic diseases. Increased antibiotic resistance and lack of effective antibiotics necessitate a search for new intervention strategies. Here we report a 3.5 Å resolution cryo-EM structure of P. gingivalis RNA polymerase (RNAP). The structure displays new structural features in its ω subunit and multiple domains in β and β' subunits, which differ from their counterparts in other bacterial RNAPs. Superimpositions with E. coli RNAP holoenzyme and initiation complex further suggest that its ω subunit may contact the σ4 domain, thereby possibly contributing to the assembly and stabilization of initiation complexes. In addition to revealing the unique features of P. gingivalis RNAP, our work offers a framework for future studies of transcription regulation in this important pathogen, as well as for structure-based drug development. PubMed: 38583515DOI: 10.1016/j.jmb.2024.168568 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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