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

Proc Natl Acad Sci U S A. 1998 Apr 28;95(9):5067-71. doi: 10.1073/pnas.95.9.5067.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Bacillus subtilis / chemistry*
  • Bacillus subtilis / genetics
  • Bacterial Proteins / physiology
  • Bacterial Proteins / ultrastructure*
  • Gene Expression Regulation, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Phosphoproteins / ultrastructure
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Sigma Factor / physiology
  • Spores, Bacterial
  • Transcription Factors*


  • Bacterial Proteins
  • Phosphoproteins
  • Sigma Factor
  • Transcription Factors
  • spoIIR protein, Bacillus subtilis
  • spore-specific proteins, Bacillus

Associated data

  • PDB/1AUZ