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7xl4

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

Structural highlights

7xl4 is a 7 chain structure with sequence from Pseudomonas aeruginosa PAO1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.86Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOB_PSEAE DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_01321]

Publication Abstract from PubMed

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 sigma factor sigma(S) (RNAP-sigma(S)). 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-sigma(S) holoenzyme, Pae RNAP-sigma(S) holoenzyme complexed with SutA, and Pae RNAP-sigma(S) transcription initiation complex comprising SutA. The structures show SutA pinches RNAP-beta protrusion and facilitates promoter unwinding by wedging RNAP-beta lobe open. Our results demonstrate that SutA clears an energetic barrier to facilitate promoter unwinding of RNAP-sigma(S) holoenzyme.

Pseudomonas aeruginosa SutA wedges RNAP lobe domain open to facilitate promoter DNA unwinding.,He D, You L, Wu X, Shi J, Wen A, Yan Z, Mu W, Fang C, Feng Y, Zhang Y Nat Commun. 2022 Jul 20;13(1):4204. doi: 10.1038/s41467-022-31871-7. PMID:35859063^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ He 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. 2022 Jul 20;13(1):4204. doi: 10.1038/s41467-022-31871-7. PMID:35859063 doi:http://dx.doi.org/10.1038/s41467-022-31871-7