8BV3
Bacillus subtilis DnaA domain III structure
Summary for 8BV3
Entry DOI | 10.2210/pdb8bv3/pdb |
Descriptor | Chromosomal replication initiator protein DnaA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, POTASSIUM ION, ... (5 entities in total) |
Functional Keywords | dnaa, dna replication, dna replication initiation, aaa+ superfamily, initiator clade, cell cycle |
Biological source | Bacillus subtilis |
Total number of polymer chains | 5 |
Total formula weight | 140335.14 |
Authors | Pintar, S.,Hubbard, J.A. (deposition date: 2022-12-01, release date: 2023-12-13, Last modification date: 2023-12-27) |
Primary citation | Pelliciari, S.,Bodet-Lefevre, S.,Fenyk, S.,Stevens, D.,Winterhalter, C.,Schramm, F.D.,Pintar, S.,Burnham, D.R.,Merces, G.,Richardson, T.T.,Tashiro, Y.,Hubbard, J.,Yardimci, H.,Ilangovan, A.,Murray, H. The bacterial replication origin BUS promotes nucleobase capture. Nat Commun, 14:8339-8339, 2023 Cited by PubMed Abstract: Genome duplication is essential for the proliferation of cellular life and this process is generally initiated by dedicated replication proteins at chromosome origins. In bacteria, DNA replication is initiated by the ubiquitous DnaA protein, which assembles into an oligomeric complex at the chromosome origin (oriC) that engages both double-stranded DNA (dsDNA) and single-stranded DNA (ssDNA) to promote DNA duplex opening. However, the mechanism of DnaA specifically opening a replication origin was unknown. Here we show that Bacillus subtilis DnaA assembles into a continuous oligomer at the site of DNA melting, extending from a dsDNA anchor to engage a single DNA strand. Within this complex, two nucleobases of each ssDNA binding motif (DnaA-trio) are captured within a dinucleotide binding pocket created by adjacent DnaA proteins. These results provide a molecular basis for DnaA specifically engaging the conserved sequence elements within the bacterial chromosome origin basal unwinding system (BUS). PubMed: 38097584DOI: 10.1038/s41467-023-43823-w PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.38 Å) |
Structure validation
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