2MT4

Solution structure of the N-terminal domain of NUSA from B. Subtilis


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

RNA polymerase-induced remodelling of NusA produces a pause enhancement complex.

Ma, C.Mobli, M.Yang, X.Keller, A.N.King, G.F.Lewis, P.J.

(2015) Nucleic Acids Res 43: 2829-2840

  • DOI: https://doi.org/10.1093/nar/gkv108
  • Primary Citation of Related Structures:  
    2LY7, 2MT4

  • 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.


  • Organizational Affiliation

    School of Environmental and Life Sciences, University of Newcastle, Callaghan, NSW 2308, Australia.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transcription termination/antitermination protein NusA124Bacillus subtilis subsp. subtilis str. 168Mutation(s): 0 
Gene Names: nusABSU16600
UniProt
Find proteins for P32727 (Bacillus subtilis (strain 168))
Explore P32727 
Go to UniProtKB:  P32727
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP32727
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 200 
  • Conformers Submitted: 20 
  • Selection Criteria: target function 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-02-18
    Type: Initial release
  • Version 1.1: 2015-03-04
    Changes: Database references
  • Version 1.2: 2015-04-01
    Changes: Database references
  • Version 1.3: 2023-06-14
    Changes: Data collection, Database references, Other