ArticleMolecular cell2008
Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding.
Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Structural snapshots of the mechanism of ATP-dependent DNA damage recognition by UvrA.Nature communications · 2025Article
- Mechanistic understanding of UvrA damage detection and lesion hand-off to UvrB in Nucleotide Excision Repair.Nature communications · 2025Article
- Structural and functional analyses of the echinomycin resistance conferring protein Ecm16 from Streptomyces lasalocidi.Scientific reports · 2023Article
- Structural and functional insights into the activation of the dual incision activity of UvrC, a key player in bacterial NER.Nucleic acids research · 2023Article
- The UvrA-like protein Ecm16 requires ATPase activity to render resistance against echinomycin.Molecular microbiology · 2022Article
- Article
- Single molecule iSCAT imaging reveals a fast, energy efficient search mode for the DNA repair protein UvrA.Nanoscale · 2022Article
- In vitro reconstitution of an efficient nucleotide excision repair system using mesophilic enzymes from Deinococcus radiodurans.Communications biology · 2022Article
- Mfd - at the crossroads of bacterial DNA repair, transcriptional regulation and molecular evolvability.Transcription · 2021Review
- A Peek Inside the Machines of Bacterial Nucleotide Excision Repair.International journal of molecular sciences · 2021Review
- Single-molecule live-cell imaging visualizes parallel pathways of prokaryotic nucleotide excision repair.Nature communications · 2020Article
- Single-molecule imaging reveals molecular coupling between transcription and DNA repair machinery in live cells.Nature communications · 2020Article
- Article
- The ATPase mechanism of UvrA2 reveals the distinct roles of proximal and distal ATPase sites in nucleotide excision repair.Nucleic acids research · 2019Article
- Understanding the coupling between DNA damage detection and UvrA's ATPase using bulk and single molecule kinetics.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Mechanism of DNA Lesion Homing and Recognition by the Uvr Nucleotide Excision Repair System.Research (Washington, D.C.) · 2019Article
- Article
- ATP-dependent conformational change in ABC-ATPase RecF serves as a switch in DNA repair.Scientific reports · 2018Article
- The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators.Nucleic acids research · 2017Article
- A tale of two cities: A tribute to Aziz Sancar's Nobel Prize in Chemistry for his molecular characterization of NER.DNA repair · 2016Article
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7 authors.
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Abstract
The nucleotide excision repair pathway corrects many structurally unrelated DNA lesions. Damage recognition in bacteria is performed by UvrA, a member of the ABC ATPase superfamily whose functional form is a dimer with four nucleotide-binding domains (NBDs), two per protomer. In the 3.2 A structure of UvrA from Bacillus stearothermophilus, we observe that the nucleotide-binding sites are formed in an intramolecular fashion and are not at the dimer interface as is typically found in other ABC ATPases. UvrA also harbors two unique domains; we show that one of these is required for interaction with UvrB, its partner in lesion recognition. In addition, UvrA contains three zinc modules, the number and ligand sphere of which differ from previously published models. Structural analysis, biochemical experiments, surface electrostatics, and sequence conservation form the basis for models of ATP-modulated dimerization, UvrA-UvrB interaction, and DNA binding during the search for lesions.
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