2ly7

From Proteopedia

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

Structural highlights

2ly7 is a 1 chain structure with sequence from Bacillus subtilis subsp. subtilis str. 168. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

RPOB_BACSU DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.

Publication Abstract from PubMed

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.

RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.,Ma C, Mobli M, Yang X, Keller AN, King GF, Lewis PJ Nucleic Acids Res. 2015 Feb 17. pii: gkv108. PMID:25690895^[1]

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

References

↑ Ma C, Mobli M, Yang X, Keller AN, King GF, Lewis PJ. RNA polymerase-induced remodelling of NusA produces a pause enhancement complex. Nucleic Acids Res. 2015 Feb 17. pii: gkv108. PMID:25690895 doi:http://dx.doi.org/10.1093/nar/gkv108