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7VF9

Cryo-EM structure of Pseudomonas aeruginosa RNAP sigmaS holoenzyme complexes

Summary for 7VF9
Entry DOI10.2210/pdb7vf9/pdb
EMDB information31948
DescriptorDNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (7 entities in total)
Functional Keywordspseudomonas aeruginosa, rna polymerase, sigmas, rnap beta lobe, closed beta lobe, holoenzyme, transcription
Biological sourcePseudomonas aeruginosa PAO1
More
Total number of polymer chains6
Total formula weight432338.07
Authors
He, D.W.,You, L.L.,Zhang, Y. (deposition date: 2021-09-10, release date: 2022-07-27, Last modification date: 2024-06-19)
Primary citationHe, D.,You, L.,Wu, X.,Shi, J.,Wen, A.,Yan, Z.,Mu, W.,Fang, C.,Feng, Y.,Zhang, Y.
Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding.
Nat Commun, 13:4204-4204, 2022
Cited by
PubMed Abstract: Pseudomonas aeruginosa (Pae) SutA adapts bacteria to hypoxia and nutrition-limited environment during chronic infection by increasing transcription activity of an RNA polymerase (RNAP) holoenzyme comprising the stress-responsive σ factor σ (RNAP-σ). SutA shows no homology to previously characterized RNAP-binding proteins. The structure and mode of action of SutA remain unclear. Here we determined cryo-EM structures of Pae RNAP-σ holoenzyme, Pae RNAP-σ holoenzyme complexed with SutA, and Pae RNAP-σ transcription initiation complex comprising SutA. The structures show SutA pinches RNAP-β protrusion and facilitates promoter unwinding by wedging RNAP-β lobe open. Our results demonstrate that SutA clears an energetic barrier to facilitate promoter unwinding of RNAP-σ holoenzyme.
PubMed: 35859063
DOI: 10.1038/s41467-022-31871-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.04 Å)
Structure validation

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건을2024-11-06부터공개중

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