1AUZ

SOLUTION STRUCTURE OF SPOIIAA, A PHOSPHORYLATABLE COMPONENT OF THE SYSTEM THAT REGULATES TRANSCRIPTION FACTOR SIGMA-F OF BACILLUS SUBTILIS, NMR, 24 STRUCTURES


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 24 
  • Selection Criteria: TARGET FUNCTION AND LEAST RESTRAINT VIOLATIONS 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Solution structure of SpoIIAA, a phosphorylatable component of the system that regulates transcription factor sigmaF of Bacillus subtilis.

Kovacs, H.Comfort, D.Lord, M.Campbell, I.D.Yudkin, M.D.

(1998) Proc Natl Acad Sci U S A 95: 5067-5071

  • DOI: https://doi.org/10.1073/pnas.95.9.5067
  • Primary Citation of Related Structures:  
    1AUZ, 1BUZ

  • PubMed Abstract: 

    The establishment of differential gene expression in sporulating Bacillus subtilis involves four protein components, one of which, SpoIIAA, undergoes phosphorylation and dephosphorylation. We have used NMR spectroscopy to determine the solution structure of the nonphosphorylated form of SpoIIAA. The structure shows a fold consisting of a four-stranded beta-sheet and four alpha-helices. Knowledge of the structure helps to account for the phenotype of several strains of B. subtilis that carry known spoIIAA mutations and should facilitate investigations of the conformational consequences of phosphorylation.


  • Organizational Affiliation

    Department of Biochemistry, Department of Biochemistry, South Parks Road, Oxford University, Oxford OX1 3QU, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
SPOIIAA116Bacillus subtilisMutation(s): 0 
Gene Names: SPOIIAA
UniProt
Find proteins for P10727 (Bacillus subtilis (strain 168))
Explore P10727 
Go to UniProtKB:  P10727
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP10727
Sequence Annotations
Expand
  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 24 
  • Selection Criteria: TARGET FUNCTION AND LEAST RESTRAINT VIOLATIONS 

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1998-07-01
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2017-11-29
    Changes: Derived calculations, Other
  • Version 1.4: 2018-08-08
    Changes: Data collection, Experimental preparation, Refinement description, Source and taxonomy