1H4Y

Structure of the Anti-Sigma Factor Antagonist SpoIIAA in its Unphosphorylated Form


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.61 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.159 

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This is version 1.2 of the entry. See complete history


Literature

Structure of the Bacillus Cell Fate Determinant Spoiiaa in Phosphorylated and Unphosphorylated Forms

Seavers, P.R.Lewis, R.J.Brannigan, J.A.Verschueren, K.H.G.Murshudov, G.N.Wilkinson, A.J.

(2001) Structure 9: 605

  • DOI: https://doi.org/10.1016/s0969-2126(01)00623-2
  • Primary Citation of Related Structures:  
    1H4X, 1H4Y, 1H4Z

  • PubMed Abstract: 

    The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase sigma factors. The activity of the first of these sigma factors, sigmaF, is restricted to the forespore although sigmaF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For sigmaF to become active, it must escape from a complex with its cognate anti-sigma factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-sigma factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of sigmaF activity and cell fate.


  • Organizational Affiliation

    Structural Biology Laboratory, Department of Chemistry, University of York, YO10 5DD, York, United Kingdom.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
ANTI-SIGMA F FACTOR ANTAGONIST
A, B
117Lysinibacillus sphaericusMutation(s): 1 
UniProt
Find proteins for O32723 (Lysinibacillus sphaericus)
Explore O32723 
Go to UniProtKB:  O32723
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupO32723
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.61 Å
  • R-Value Free: 0.214 
  • R-Value Work: 0.159 
  • Space Group: P 21 21 21
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 36.764α = 90
b = 53.543β = 90
c = 101.34γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
DENZOdata reduction
SCALEPACKdata scaling
SOLVEphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2001-07-06
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance