1EY1

SOLUTION STRUCTURE OF ESCHERICHIA COLI NUSB


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 40 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the lowest energy 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

The structure of the transcriptional antiterminator NusB from Escherichia coli.

Altieri, A.S.Mazzulla, M.J.Horita, D.A.Coats, R.H.Wingfield, P.T.Das, A.Court, D.L.Byrd, R.A.

(2000) Nat Struct Biol 7: 470-474

  • DOI: https://doi.org/10.1038/75869
  • Primary Citation of Related Structures:  
    1EY1

  • PubMed Abstract: 

    We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coli. The structure reveals a novel, all alpha-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coli NusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coli NusB reported earlier.


  • Organizational Affiliation

    Structural Biophysics Laboratory, National Cancer Institute-FCRDC, Frederick, MD 21702, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ANTITERMINATION FACTOR NUSB139Escherichia coliMutation(s): 0 
UniProt
Find proteins for P0A780 (Escherichia coli (strain K12))
Explore P0A780 
Go to UniProtKB:  P0A780
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP0A780
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 40 
  • Conformers Submitted: 15 
  • Selection Criteria: structures with the lowest energy 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-06-14
    Type: Initial release
  • Version 1.1: 2008-04-27
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2022-02-16
    Changes: Database references, Derived calculations
  • Version 1.4: 2022-06-15
    Changes: Structure summary