8BTG
Cryo-EM structure of the bacterial replication origin opening basal unwinding system
Summary for 8BTG
Entry DOI | 10.2210/pdb8btg/pdb |
EMDB information | 16229 |
Descriptor | Chromosomal replication initiator protein DnaA, DNA (5'-D(P*AP*CP*TP*TP*AP*TP*CP*CP*AP*CP*AP*AP*AP*TP*CP*CP*AP*CP*AP*GP*GP*CP*CP*C)-3'), DNA (41-MER), ... (5 entities in total) |
Functional Keywords | dnaa, cryo-em, bus complex, replication initiation, replication |
Biological source | Bacillus subtilis More |
Total number of polymer chains | 9 |
Total formula weight | 380313.23 |
Authors | Pelliciari, S.,Bodet-Lefevre, S.,Murray, H.,Ilangovan, A. (deposition date: 2022-11-28, release date: 2024-02-14) |
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-, 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: 10.1093/nar/gkac1060 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.2 Å) |
Structure validation
Download full validation report