5OND

RfaH from Escherichia coli in complex with ops DNA

Summary for 5OND

• Entry DOI: 10.2210/pdb5ond/pdb
• Descriptor: Transcription antitermination protein RfaH, DNA (5'-D(*GP*CP*GP*GP*TP*AP*GP*TP*C)-3') (3 entities in total)
• Functional Keywords: operon-specific transcription factor, transformer protein, binding of single stranded dna, translation activation, transcription
• Biological source: Escherichia coli; More
• Total number of polymer chains: 4
• Total formula weight: 42187.92

Authors

Zuber, P.K.,Artsimovitch, I.,Roesch, P.,Knauer, S.H. (deposition date: 2017-08-03, release date: 2018-06-06, Last modification date: 2024-01-17)

Primary citation

Zuber, P.K.,Artsimovitch, I.,NandyMazumdar, M.,Liu, Z.,Nedialkov, Y.,Schweimer, K.,Rosch, P.,Knauer, S.H.
The universally-conserved transcription factor RfaH is recruited to a hairpin structure of the non-template DNA strand.
Elife, 7:-, 2018

PubMed Abstract: RfaH, a transcription regulator of the universally conserved NusG/Spt5 family, utilizes a unique mode of recruitment to elongating RNA polymerase to activate virulence genes. RfaH function depends critically on an sequence, an exemplar of a consensus pause, in the non-template DNA strand of the transcription bubble. We used structural and functional analyses to elucidate the role of in RfaH recruitment. Our results demonstrate that induces pausing to facilitate RfaH binding and establishes direct contacts with RfaH. Strikingly, the non-template DNA forms a hairpin in the RfaH: complex structure, flipping out a conserved T residue that is specifically recognized by RfaH. Molecular modeling and genetic evidence support the notion that hairpin is required for RfaH recruitment. We argue that both the sequence and the structure of the non-template strand are read out by transcription factors, expanding the repertoire of transcriptional regulators in all domains of life.

PubMed: 29741479
DOI: 10.7554/eLife.36349

Experimental method

X-RAY DIFFRACTION (2.1 Å)