Member database | Pfam |
Pfam type | domain |
Short name | Sda |
Author | Mistry J;0000-0003-2479-5322 Sammut SJ;0000-0003-4472-904X |
Sequence Ontology | 0000417 |
Description
Members of this protein family contain two antiparallel alpha helices that are linked by a highly structured inter-helix loop to form a helical hairpin; the structure is stabilised by numerous hydrophobic and electrostatic interactions. These sporulation inhibitors are antikinases that bind to the histidine kinase KinA phosphotransfer domain and act as a molecular barricade that inhibit productive interaction between the ATP binding site and the phosphorylatable KinA His residue. This results in the inhibition of sporulation (by preventing phosphorylation of spo0A)
[1].
References
1.Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis. Rowland SL, Burkholder WF, Cunningham KA, Maciejewski MW, Grossman AD, King GF. Mol. Cell 13, 689-701, (2004). View articlePMID: 15023339
Integrated to
Representative structure
3fyr: Crystal structure of the sporulation histidine kinase inhibitor Sda from Bacillus subtilis