2HCB

Structure of AMPPCP-bound DnaA from Aquifex aeolicus

Summary for 2HCB

• Entry DOI: 10.2210/pdb2hcb/pdb
• Descriptor: Chromosomal replication initiator protein dnaA, MAGNESIUM ION, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER (3 entities in total)
• Functional Keywords: aaa+ atpase, helix-turn-helix, replication
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm: O66659
• Total number of polymer chains: 4
• Total formula weight: 153049.27

Authors

Erzberger, J.P.,Mott, M.L.,Berger, J.M. (deposition date: 2006-06-15, release date: 2006-07-25, Last modification date: 2023-08-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.51 Å)