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7XL3

Cryo-EM structure of Pseudomonas aeruginosa RNAP sigmaS holoenzyme complexes with transcription factor SutA (open lobe)

Summary for 7XL3
Entry DOI10.2210/pdb7xl3/pdb
EMDB information33271
DescriptorDNA-directed RNA polymerase subunit alpha, DNA-directed RNA polymerase subunit beta, DNA-directed RNA polymerase subunit beta', ... (8 entities in total)
Functional Keywordstranscription initiation, pseudomonas aeruginosa, rna polymerase, sigmas, suta, rnap beta lobe, open beta lobe, transcription
Biological sourcePseudomonas aeruginosa PAO1
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Total number of polymer chains7
Total formula weight443835.44
Authors
He, D.W.,You, L.L.,Zhang, Y. (deposition date: 2022-04-21, release date: 2022-07-27, Last modification date: 2024-07-03)
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 (3.13 Å)
Structure validation

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