7BEG
Structures of class I bacterial transcription complexes
Summary for 7BEG
| Entry DOI | 10.2210/pdb7beg/pdb |
| EMDB information | 12157 |
| Descriptor | DNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total) |
| Functional Keywords | antibiotic resistance, bacterial transcription activator, cryoem, transcription |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 9 |
| Total formula weight | 535386.84 |
| Authors | Ye, F.Z.,Hao, M.,Zhang, X.D. (deposition date: 2020-12-23, release date: 2021-12-01, Last modification date: 2024-07-10) |
| Primary citation | Hao, M.,Ye, F.,Jovanovic, M.,Kotta-Loizou, I.,Xu, Q.,Qin, X.,Buck, M.,Zhang, X.,Wang, M. Structures of Class I and Class II Transcription Complexes Reveal the Molecular Basis of RamA-Dependent Transcription Activation. Adv Sci, 9:e2103669-e2103669, 2022 Cited by PubMed Abstract: Transcription activator RamA is linked to multidrug resistance of Klebsiella pneumoniae through controlling genes that encode efflux pumps (acrA) and porin-regulating antisense RNA (micF). In bacteria, σ , together with activators, controls the majority of genes by recruiting RNA polymerase (RNAP) to the promoter regions. RNAP and σ form a holoenzyme that recognizes -35 and -10 promoter DNA consensus sites. Many activators bind upstream from the holoenzyme and can be broadly divided into two classes. RamA acts as a class I activator on acrA and class II activator on micF, respectively. The authors present biochemical and structural data on RamA in complex with RNAP-σ at the two promoters and the data reveal the molecular basis for how RamA assembles and interacts with core RNAP and activates transcription that contributes to antibiotic resistance. Further, comparing with CAP/TAP complexes reveals common and activator-specific features in activator binding and uncovers distinct roles of the two C-terminal domains of RNAP α subunit. PubMed: 34761556DOI: 10.1002/advs.202103669 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.2 Å) |
Structure validation
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