1L8Q

CRYSTAL STRUCTURE OF DNA REPLICATION INITIATION FACTOR

Summary for 1L8Q

• Entry DOI: 10.2210/pdb1l8q/pdb
• Descriptor: Chromosomal replication initiator protein dnaA, MAGNESIUM ION, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: aaa+, helix-turn-helix, nucleotide-binding, dna binding, replication initiation, dna binding protein
• Biological source: Aquifex aeolicus
• Cellular location: Cytoplasm: O66659
• Total number of polymer chains: 1
• Total formula weight: 38501.07

Authors

Erzberger, J.P.,Pirruccello, M.M.,Berger, J.M. (deposition date: 2002-03-21, release date: 2002-09-25, Last modification date: 2024-11-13)

Primary citation

Erzberger, J.P.,Pirruccello, M.M.,Berger, J.M.
The structure of bacterial DnaA: implications for general mechanisms underlying DNA replication initiation
Embo J., 21:4763-4773, 2002

PubMed Abstract: The initiation of DNA replication is a key event in the cell cycle of all organisms. In bacteria, replication initiation occurs at specific origin sequences that are recognized and processed by an oligomeric complex of the initiator protein DnaA. We have determined the structure of the conserved core of the Aquifex aeolicus DnaA protein to 2.7 A resolution. The protein comprises an AAA+ nucleotide-binding fold linked through a long, helical connector to an all-helical DNA-binding domain. The structure serves as a template for understanding the physical consequences of a variety of DnaA mutations, and conserved motifs in the protein suggest how two critical aspects of origin processing, DNA binding and homo-oligomerization, are mediated. The spatial arrangement of these motifs in DnaA is similar to that of the eukaryotic-like archaeal replication initiation factor Cdc6/Orc1, demonstrating that mechanistic elements of origin processing may be conserved across bacterial, archaeal and eukaryotic domains of life.

PubMed: 12234917
DOI: 10.1093/emboj/cdf496

Experimental method

X-RAY DIFFRACTION (2.7 Å)