ArticleNucleic acids research2010
The structure of DdrB from Deinococcus: a new fold for single-stranded DNA binding proteins.
Article in Nucleic acids research, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.Nucleic acids research · 2026Article
- Mechanism of single-strand annealing from native mass spectrometry and cryo-EM structures of RAD52 homolog Mgm101.bioRxiv : the preprint server for biology · 2025Article
- Surviving the storm: exploring the role of natural transformation in nutrition and DNA repair of stressedApplied and environmental microbiology · 2025Article
- Mutational Analysis of Redβ Single Strand Annealing Protein: Roles of the 14 Lysine Residues in DNA Binding and Recombination In Vivo.International journal of molecular sciences · 2021Article
- Structural features and functional implications of proteins enabling the robustness ofComputational and structural biotechnology journal · 2020Review
- Conservation and diversity of radiation and oxidative stress resistance mechanisms in Deinococcus species.FEMS microbiology reviews · 2019Review
- Mechanism for accurate, protein-assisted DNA annealing by Deinococcus radiodurans DdrB.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- A Decade of Biochemical and Structural Studies of the DNA Repair Machinery ofComputational and structural biotechnology journal · 2016Review
- Single Strand Annealing Plays a Major Role in RecA-Independent Recombination between Repeated Sequences in the Radioresistant Deinococcus radiodurans Bacterium.PLoS genetics · 2015Article
- Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprA.Nucleic acids research · 2014Article
- C-terminal domain swapping of SSB changes the size of the ssDNA binding site.BioMed research international · 2014Article
- Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric states.Nucleic acids research · 2013Article
- Structures of apo- and ssDNA-bound YdbC from Lactococcus lactis uncover the function of protein domain family DUF2128 and expand the single-stranded DNA-binding domain proteome.Nucleic acids research · 2013Article
- Major soluble proteome changes in Deinococcus deserti over the earliest stages following gamma-ray irradiation.Proteome science · 2013Article
- Article
- The essential role of the Deinococcus radiodurans ssb gene in cell survival and radiation tolerance.PloS one · 2013Article
- Crystallization of the DdrB-DNA complex from Deinococcus radiodurans.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
- Structure and cellular dynamics of Deinococcus radiodurans single-stranded DNA (ssDNA)-binding protein (SSB)-DNA complexes.The Journal of biological chemistry · 2012Article
- Displacement of the canonical single-stranded DNA-binding protein in the Thermoproteales.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Gamma radiation-induced proteome of Deinococcus radiodurans primarily targets DNA repair and oxidative stress alleviation.Molecular & cellular proteomics : MCP · 2012Article
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2 authors.
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Abstract
Deinococcus spp. are renowned for their amazing ability to recover rapidly from severe genomic fragmentation as a result of exposure to extreme levels of ionizing radiation or desiccation. Despite having been originally characterized over 50 years ago, the mechanism underlying this remarkable repair process is still poorly understood. Here, we report the 2.8 A structure of DdrB, a single-stranded DNA (ssDNA) binding protein unique to Deinococcus spp. that is crucial for recovery following DNA damage. DdrB forms a pentameric ring capable of binding single-stranded but not double-stranded DNA. Unexpectedly, the crystal structure reveals that DdrB comprises a novel fold that is structurally and topologically distinct from all other single-stranded binding (SSB) proteins characterized to date. The need for a unique ssDNA binding function in response to severe damage, suggests a distinct role for DdrB which may encompass not only standard SSB protein function in protection of ssDNA, but also more specialized roles in protein recruitment or DNA architecture maintenance. Possible mechanisms of DdrB action in damage recovery are discussed.
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