3C1Y

Structure of bacterial DNA damage sensor protein with co-purified and co-crystallized ligand

3C1Y の概要

• エントリーDOI: 10.2210/pdb3c1y/pdb
• 関連するPDBエントリー: 3C1Z 3C21 3C23
• 分子名称: DNA integrity scanning protein disA, (2R,3R,3aS,5R,7aR,9R,10R,10aS,12R,14aR)-2,9-bis(6-amino-9H-purin-9-yl)octahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8 ]tetraoxadiphosphacyclododecine-3,5,10,12-tetrol 5,12-dioxide (3 entities in total)
• 機能のキーワード: dna damage, dna repair, dna-binding, dna binding protein
• 由来する生物種: Thermotoga maritima
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86186.38

構造登録者

Witte, G.,Hartung, S.,Buttner, K.,Hopfner, K.P. (登録日: 2008-01-24, 公開日: 2008-05-06, 最終更新日: 2024-03-13)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)