|PDB structures||RCSB PDB PDBe PDBsum|
Diadenylate cyclase EC 184.108.40.206, DNA integrity scanning protein DisA is a DNA binding protein participates in a DNA-damage check-point. DisA forms globular foci that rapidly scan along the chromosomes searching for lesions. Catalytic activity
- 2 ATP 2 diphosphate + cyclic di-3',5'-adenylate.
This enzyme has diadenylate cyclase activity, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP). c-di-AMP likely acts as a signaling molecule that may couple DNA integrity with a cellular process. This rate-limiting step is the accessibility of the active site; mutating the possible exit tunnel (residues 128-130) increases product 2-fold despite Arg-130 being important for ATP-binding. Does not convert GTP to c-di-GMP.
- Witte G, Hartung S, Büttner K, Hopfner KP (April 2008). "Structural biochemistry of a bacterial checkpoint protein reveals diadenylate cyclase activity regulated by DNA recombination intermediates". Molecular Cell. 30 (2): 167–78. doi:10.1016/j.molcel.2008.02.020. PMID 18439896.