2LY7

B-flap domain of RNA polymerase (B. subtilis)

Summary for 2LY7

• Entry DOI: 10.2210/pdb2ly7/pdb
• NMR Information: BMRB: 18712
• Descriptor: DNA-directed RNA polymerase subunit beta (1 entity in total)
• Functional Keywords: rna polymerase, transcription, non-uniform sampling
• Biological source: Bacillus subtilis
• Total number of polymer chains: 1
• Total formula weight: 16679.60

Authors

Mobli, M. (deposition date: 2012-09-12, release date: 2014-03-12, Last modification date: 2024-05-15)

Primary citation

Ma, C.,Mobli, M.,Yang, X.,Keller, A.N.,King, G.F.,Lewis, P.J.
RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.
Nucleic Acids Res., 43:2829-2840, 2015

PubMed Abstract: Pausing during transcription elongation is a fundamental activity in all kingdoms of life. In bacteria, the essential protein NusA modulates transcriptional pausing, but its mechanism of action has remained enigmatic. By combining structural and functional studies we show that a helical rearrangement induced in NusA upon interaction with RNA polymerase is the key to its modulatory function. This conformational change leads to an allosteric re-positioning of conserved basic residues that could enable their interaction with an RNA pause hairpin that forms in the exit channel of the polymerase. This weak interaction would stabilize the paused complex and increases the duration of the transcriptional pause. Allosteric spatial re-positioning of regulatory elements may represent a general approach used across all taxa for modulation of transcription and protein-RNA interactions.

PubMed: 25690895
DOI: 10.1093/nar/gkv108

Experimental method

SOLUTION NMR