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8BV3

Bacillus subtilis DnaA domain III structure

Summary for 8BV3
Entry DOI10.2210/pdb8bv3/pdb
DescriptorChromosomal replication initiator protein DnaA, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, POTASSIUM ION, ... (5 entities in total)
Functional Keywordsdnaa, dna replication, dna replication initiation, aaa+ superfamily, initiator clade, cell cycle
Biological sourceBacillus subtilis
Total number of polymer chains5
Total formula weight140335.14
Authors
Pintar, S.,Hubbard, J.A. (deposition date: 2022-12-01, release date: 2023-12-13, Last modification date: 2023-12-27)
Primary citationPelliciari, 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: 38097584
DOI: 10.1038/s41467-023-43823-w
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.38 Å)
Structure validation

243083

数据于2025-10-15公开中

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