2HCB

Structure of AMPPCP-bound DnaA from Aquifex aeolicus

2HCB の概要

• エントリーDOI: 10.2210/pdb2hcb/pdb
• 分子名称: Chromosomal replication initiator protein dnaA, MAGNESIUM ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: aaa+ atpase, helix-turn-helix, replication
• 由来する生物種: Aquifex aeolicus
• 細胞内の位置: Cytoplasm: O66659
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153049.27

構造登録者

Erzberger, J.P.,Mott, M.L.,Berger, J.M. (登録日: 2006-06-15, 公開日: 2006-07-25, 最終更新日: 2023-08-30)

主引用文献

Erzberger, J.P.,Mott, M.L.,Berger, J.M.
Structural basis for ATP-dependent DnaA assembly and replication-origin remodeling.
Nat.Struct.Mol.Biol., 13:676-683, 2006

PubMed Abstract: In bacteria, the initiation of replication is controlled by DnaA, a member of the ATPases associated with various cellular activities (AAA+) protein superfamily. ATP binding allows DnaA to transition from a monomeric state into a large oligomeric complex that remodels replication origins, triggers duplex melting and facilitates replisome assembly. The crystal structure of AMP-PCP-bound DnaA reveals a right-handed superhelix defined by specific protein-ATP interactions. The observed quaternary structure of DnaA, along with topology footprint assays, indicates that a right-handed DNA wrap is formed around the initiation nucleoprotein complex. This model clarifies how DnaA engages and unwinds bacterial origins and suggests that additional, regulatory AAA+ proteins engage DnaA at filament ends. Eukaryotic and archaeal initiators also have the structural elements that promote open-helix formation, indicating that a spiral, open-ring AAA+ assembly forms the core element of initiators in all domains of life.

PubMed: 16829961
DOI: 10.1038/nsmb1115

実験手法

X-RAY DIFFRACTION (3.51 Å)