2MT4
Solution structure of the N-terminal domain of NUSA from B. Subtilis
Summary for 2MT4
| Entry DOI | 10.2210/pdb2mt4/pdb |
| NMR Information | BMRB: 25148 |
| Descriptor | Transcription termination/antitermination protein NusA (1 entity in total) |
| Functional Keywords | transcription factor, nusa, rna polymerase, transcription |
| Biological source | Bacillus subtilis |
| Cellular location | Cytoplasm : P32727 |
| Total number of polymer chains | 1 |
| Total formula weight | 14019.86 |
| Authors | Mobli, M.,Lewis, P.J. (deposition date: 2014-08-12, release date: 2015-02-18, 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 Cited by 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: 25690895DOI: 10.1093/nar/gkv108 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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