3C23

Structure of a bacterial DNA damage sensor protein with non-reactive Ligand

Summary for 3C23

• Entry DOI: 10.2210/pdb3c23/pdb
• Related: 3C1Y 3C1Z 3C21
• Descriptor: DNA integrity scanning protein disA, 3'-DEOXYADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• Functional Keywords: dna damage, dna repair, dna-binding, dna binding protein
• Biological source: Thermotoga maritima
• Total number of polymer chains: 2
• Total formula weight: 86510.33

Authors

Witte, G.,Hartung, S.,Buttner, K.,Hopfner, K.P. (deposition date: 2008-01-24, release date: 2008-05-06, Last modification date: 2023-11-01)

Primary citation

Witte, G.,Hartung, S.,Buttner, K.,Hopfner, K.P.
Structural Biochemistry of a Bacterial Checkpoint Protein Reveals Diadenylate Cyclase Activity Regulated by DNA Recombination Intermediates
Mol.Cell, 30:167-178, 2008

PubMed Abstract: To reveal mechanisms of DNA damage checkpoint initiation, we structurally and biochemically analyzed DisA, a protein that controls a Bacillus subtilis sporulation checkpoint in response to DNA double-strand breaks. We find that DisA forms a large octamer that consists of an array of an uncharacterized type of nucleotide-binding domain along with two DNA-binding regions related to the Holliday junction recognition protein RuvA. Remarkably, the nucleotide-binding domains possess diadenylate cyclase activity. The resulting cyclic diadenosine phosphate, c-di-AMP, is reminiscent but distinct from c-di-GMP, an emerging prokaryotic regulator of complex cellular processes. Diadenylate cyclase activity is unaffected by linear DNA or DNA ends but strongly suppressed by branched nucleic acids such as Holliday junctions. Our data indicate that DisA signals DNA structures that interfere with chromosome segregation via c-di-AMP. Identification of the diadenylate cyclase domain in other eubacterial and archaeal proteins implies a more general role for c-di-AMP in prokaryotes.

PubMed: 18439896
DOI: 10.1016/j.molcel.2008.02.020

Experimental method

X-RAY DIFFRACTION (2.5 Å)