10YO

Nocardia pseudobrasiliensis DnaA DI

10YO の概要

• エントリーDOI: 10.2210/pdb10yo/pdb
• 分子名称: Chromosomal replication initiator protein DnaA, PHOSPHATE ION (3 entities in total)
• 機能のキーワード: initiator, dna binding protein
• 由来する生物種: Nocardia pseudobrasiliensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10591.91

構造登録者

Chavez Orozco, J.G.,Ellis, P.K.,Schumacher, M.A. (登録日: 2026-02-12, 公開日: 2026-06-03, 最終更新日: 2026-07-01)

主引用文献

Ellis, P.K.,Srinivasu, B.Y.,Chavez Orozco Jr., J.,Wray, G.A.,Wales, T.E.,Schumacher, M.A.
Structures of DnaA domain I reveal a dimer conserved across Actinomycetes.
Nucleic Acids Res., 54:-, 2026

PubMed Abstract: DNA replication is a fundamental process in biology, and initiation marks a key regulatory step. In bacteria, DNA replication is initiated by the DnaA protein. DnaA exhibits multidomain architecture, consisting of an N-terminal domain I, linker region, AAA+ family ATPase cassette, and C-terminal DNA-binding motif. Taxon-specific regulatory functions are primarily coordinated by the DnaA domain I (DnaADI), which exhibits substantial sequence variation across bacteria. Notably, although DnaADI has been shown to be essential, its contributions to initiation are not completely understood. Previous studies suggested a role for DnaADI in the assembly of the initiation complex at the origin. However, the molecular mechanisms behind DnaADI functions have not been resolved. Here, we report the DnaADI structures from 10 species in the class Actinomycetes. Strikingly, all structures reveal the same, unique dimer, and our analyses show that key elements that support DnaADI self-interaction are broadly conserved across the class Actinomycetes. Further, a suite of biochemical oligomerization assays and HDX-MS (hydrogen-deuterium exchange mass spectrometry) studies support the formation of dimers with µM affinities. These findings suggest that weak DnaADI dimerization, which is a broadly conserved mechanism across the Actinomycetes, likely contributes to proper replication initiation in these bacteria.

PubMed: 42301917
DOI: 10.1093/nar/gkag596

実験手法

X-RAY DIFFRACTION (2.8 Å)