1H4X

Structure of the Bacillus Cell Fate Determinant SpoIIAA in the Phosphorylated Form

Summary for 1H4X

• Entry DOI: 10.2210/pdb1h4x/pdb
• Descriptor: ANTI-SIGMA F FACTOR ANTAGONIST, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL (3 entities in total)
• Functional Keywords: cell differentiation, phosphorylation, sigma factor, sporulation
• Biological source: BACILLUS SPHAERICUS
• Total number of polymer chains: 2
• Total formula weight: 26654.69

Authors

Seavers, P.R.,Lewis, R.J.,Brannigan, J.A.,Verschueren, K.H.G.,Murshudov, G.N.,Wilkinson, A.J. (deposition date: 2001-05-15, release date: 2001-07-06, Last modification date: 2024-10-16)

Primary citation

Seavers, P.R.,Lewis, R.J.,Brannigan, J.A.,Verschueren, K.H.G.,Murshudov, G.N.,Wilkinson, A.J.
Structure of the Bacillus Cell Fate Determinant Spoiiaa in Phosphorylated and Unphosphorylated Forms
Structure, 9:605-, 2001

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.

PubMed: 11470435
DOI: 10.1016/S0969-2126(01)00623-2

Experimental method

X-RAY DIFFRACTION (1.16 Å)