3T9Q

Structure of the Phosphatase Domain of the Cell Fate Determinant SpoIIE from Bacillus subtilis (Mn presoaked)

Summary for 3T9Q

• Entry DOI: 10.2210/pdb3t9q/pdb
• Related: 3T91
• Descriptor: Stage II sporulation protein E, MANGANESE (II) ION, beta-D-gulopyranose, ... (4 entities in total)
• Functional Keywords: spoiie, phosphatase, sporulation, manganese binding, pp2c phosphatase domain, dephosphorylating the anti-sigma factor antagonist spoiiaa, hydrolase
• Biological source: Bacillus subtilis
• Cellular location: Cell membrane; Multi-pass membrane protein (By similarity): P37475
• Total number of polymer chains: 2
• Total formula weight: 53370.88

Authors

Levdikov, V.M.,Blagova, E.V.,Wilkinson, A.J. (deposition date: 2011-08-03, release date: 2011-12-07, Last modification date: 2023-09-13)

Primary citation

Levdikov, V.M.,Blagova, E.V.,Rawlings, A.E.,Jameson, K.,Tunaley, J.,Hart, D.J.,Barak, I.,Wilkinson, A.J.
Structure of the phosphatase domain of the cell fate determinant SpoIIE from Bacillus subtilis.
J.Mol.Biol., 415:343-358, 2012

PubMed Abstract: Sporulation in Bacillus subtilis begins with an asymmetric cell division producing two genetically identical cells with different fates. SpoIIE is a membrane protein that localizes to the polar cell division sites where it causes FtsZ to relocate from mid-cell to form polar Z-rings. Following polar septation, SpoIIE establishes compartment-specific gene expression in the smaller forespore cell by dephosphorylating the anti-sigma factor antagonist SpoIIAA, leading to the release of the RNA polymerase sigma factor σ(F) from an inhibitory complex with the anti-sigma factor SpoIIAB. SpoIIE therefore couples morphological development to differential gene expression. Here, we determined the crystal structure of the phosphatase domain of SpoIIE to 2.6 Å spacing, revealing a domain-swapped dimer. SEC-MALLS (size-exclusion chromatography with multi-angle laser light scattering) analysis however suggested a monomer as the principal form in solution. A model for the monomer was derived from the domain-swapped dimer in which 2 five-stranded β-sheets are packed against one another and flanked by α-helices in an αββα arrangement reminiscent of other PP2C-type phosphatases. A flap region that controls access of substrates to the active site in other PP2C phosphatases is diminished in SpoIIE, and this observation correlates with the presence of a single manganese ion in the active site of SpoIIE in contrast to the two or three metal ions present in other PP2C enzymes. Mapping of a catalogue of mutational data onto the structure shows a clustering of sites whose point mutation interferes with the proper coupling of asymmetric septum formation to sigma factor activation and identifies a surface involved in intramolecular signaling.

PubMed: 22115775
DOI: 10.1016/j.jmb.2011.11.017

Experimental method

X-RAY DIFFRACTION (2.76 Å)