ArticlePloS one2022
X-ray crystal structure of the Escherichia coli RadD DNA repair protein bound to ADP reveals a novel zinc ribbon domain.
Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed.
- PrgE: an OB-fold protein from plasmid pCF10 with striking differences to prototypical bacterial SSBs.Life science alliance · 2024Article
- Generation and Repair of Postreplication Gaps in Escherichia coli.Microbiology and molecular biology reviews : MMBR · 2023Review
- Biochemical and Structural Analyses Shed Light on the Mechanisms of RadD DNA Binding and Its ATPase fromInternational journal of molecular sciences · 2023Article
- Molecular insights into the prototypical single-stranded DNA-binding protein fromCritical reviews in biochemistry and molecular biologyReview
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4 authors.
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Abstract
Genome maintenance is an essential process in all cells. In prokaryotes, the RadD protein is important for survival under conditions that include DNA-damaging radiation. Precisely how RadD participates in genome maintenance remains unclear. Here we present a high-resolution X-ray crystal structure of ADP-bound Escherichia coli RadD, revealing a zinc-ribbon element that was not modelled in a previous RadD crystal structure. Insights into the mode of nucleotide binding and additional structure refinement afforded by the new RadD model will help to drive investigations into the activity of RadD as a genome stability and repair factor.
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