ArticleNucleic acids research2014
Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- A Single DNA Binding Site of DprA Dimer Is Required to Facilitate RecA Filament Nucleation.International journal of molecular sciences · 2025Article
- Article
- The Lonely Guy (LOG) Homologue SiRe_0427 from the Thermophilic ArchaeonApplied and environmental microbiology · 2019Article
- DprA Is Essential for Natural Competence inFrontiers in genetics · 2019Article
- DprA from Neisseria meningitidis: properties and role in natural competence for transformation.Microbiology (Reading, England) · 2017Article
- Mutations in the nucleotide binding and hydrolysis domains of Helicobacter pylori MutS2 lead to altered biochemical activities and inactivation of its in vivo function.BMC microbiology · 2016Article
- Genome Sequence of Mycobacteriophage Mindy.Genome announcements · 2015Article
- Insights into the Functional Roles of N-Terminal and C-Terminal Domains of Helicobacter pylori DprA.PloS one · 2015Article
- Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic recombination.The Journal of biological chemistry · 2014Article
- Evidence that the C-terminal domain of a type B PutA protein contributes to aldehyde dehydrogenase activity and substrate channeling.Biochemistry · 2014Article
- Crystal structure of DnaT84-153-dT10 ssDNA complex reveals a novel single-stranded DNA binding mode.Nucleic acids research · 2014Article
- Molecular determinants of the DprA-RecA interaction for nucleation on ssDNA.Nucleic acids research · 2014Article
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5 authors.
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Abstract
Natural transformation (NT) in bacteria is a complex process, including binding, uptake, transport and recombination of exogenous DNA into the chromosome, consequently generating genetic diversity and driving evolution. DNA processing protein A (DprA), which is distributed among virtually all bacterial species, is involved in binding to the internalized single-stranded DNA (ssDNA) and promoting the loading of RecA on ssDNA during NTs. Here we present the structures of DNA_processg_A (DprA) domain of the Helicobacter pylori DprA (HpDprA) and its complex with an ssDNA at 2.20 and 1.80 Å resolutions, respectively. The complex structure revealed for the first time how the conserved DprA domain binds to ssDNA. Based on structural comparisons and binding assays, a unique ssDNA-binding mode is proposed: the dimer of HpDprA binds to ssDNA through two small, positively charged binding pockets of the DprA domains with classical Rossmann folds and the key residue Arg52 is re-oriented to 'open' the pocket in order to accommodate one of the bases of ssDNA, thus enabling HpDprA to grasp substrate with high affinity. This mode is consistent with the oligomeric composition of the complex as shown by electrophoretic mobility-shift assays and static light scattering measurements, but differs from the direct polymeric complex of Streptococcus pneumoniae DprA-ssDNA.
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