ArticleNucleic acids research2019
Sharp kinking of a coiled-coil in MutS allows DNA binding and release.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Molecular dynamics of mismatch detection-How MutS uses indirect readout to find errors in DNA.Biophysical journal · 2023Article
- Likelihood-based docking of models into cryo-EM maps.Acta crystallographica. Section D, Structural biology · 2023Article
- Nanobodies and chemical cross-links advance the structural and functional analysis of PI3Kα.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bioinformatics Analysis of the Periodicity in Proteins with Coiled-Coil Structure-Enumerating All Decompositions of Sequence Periods.International journal of molecular sciences · 2022Article
- Reactive Acrylamide-Modified DNA Traps for Accurate Cross-Linking with Cysteine Residues in DNA-Protein Complexes Using Mismatch Repair Protein MutS as a Model.Molecules (Basel, Switzerland) · 2022Article
- Single-Molecule Methods for Investigating the Double-Stranded DNA Bendability.Molecules and cells · 2022Review
- Atomistic basis of force generation, translocation, and coordination in a viral genome packaging motor.Nucleic acids research · 2021Article
- The selection process of licensing a DNA mismatch for repair.Nature structural & molecular biology · 2021Article
- Recurrent mismatch binding by MutS mobile clamps on DNA localizes repair complexes nearby.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Exploring the Binding Mechanism and Dynamics of EndoMS/NucS to Mismatched dsDNA.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
DNA mismatch repair (MMR) corrects mismatches, small insertions and deletions in DNA during DNA replication. While scanning for mismatches, dimers of MutS embrace the DNA helix with their lever and clamp domains. Previous studies indicated generic flexibility of the lever and clamp domains of MutS prior to DNA binding, but whether this was important for MutS function was unknown. Here, we present a novel crystal structure of DNA-free Escherichia coli MutS. In this apo-structure, the clamp domains are repositioned due to kinking at specific sites in the coiled-coil region in the lever domains, suggesting a defined hinge point. We made mutations at the coiled-coil hinge point. The mutants made to disrupt the helical fold at the kink site diminish DNA binding, whereas those made to increase stability of coiled-coil result in stronger DNA binding. These data suggest that the site-specific kinking of the coiled-coil in the lever domain is important for loading of this ABC-ATPase on DNA.
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