7xya

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The cryo-EM structure of an AlpA-loading complexThe cryo-EM structure of an AlpA-loading complex

Structural highlights

7xya is a 10 chain structure with sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Electron Microscopy, Resolution 3.3Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOA_PSEAE DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.[HAMAP-Rule:MF_00059]

Publication Abstract from PubMed

AlpA positively regulates a programmed cell death pathway linked to the virulence of Pseudomonas aeruginosa by recognizing an AlpA binding element within the promoter, then binding RNA polymerase directly and allowing it to bypass an intrinsic terminator positioned downstream. Here, we report the single-particle cryo-electron microscopy structures of both an AlpA-loading complex and an AlpA-loaded complex. These structures indicate that the C-terminal helix-turn-helix motif of AlpA binds to the AlpA binding element and that the N-terminal segment of AlpA forms a narrow ring inside the RNA exit channel. AlpA was also revealed to render RNAP resistant to termination signals by prohibiting RNA hairpin formation in the RNA exit channel. Structural analysis predicted that AlpA, 21Q, lambdaQ and 82Q share the same mechanism of transcription antitermination.

Structural basis of AlpA-dependent transcription antitermination.,Wen A, Zhao M, Jin S, Lu YQ, Feng Y Nucleic Acids Res. 2022 Aug 12;50(14):8321-8330. doi: 10.1093/nar/gkac608. PMID:35871295[1]

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

See Also

References

  1. Wen A, Zhao M, Jin S, Lu YQ, Feng Y. Structural basis of AlpA-dependent transcription antitermination. Nucleic Acids Res. 2022 Aug 12;50(14):8321-8330. doi: 10.1093/nar/gkac608. PMID:35871295 doi:http://dx.doi.org/10.1093/nar/gkac608

7xya, resolution 3.30Å

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OCA