Abstract
DNA mismatch repair (MMR) is initiated when the MutS protein recognizes damaged DNA. Crystal structures of MutS bound to mispaired and unpaired DNA show how MutS distinguishes damaged from undamaged DNA and explain how a broad variety of DNA mismatch lesions can be detected. The structures suggest mechanisms for the ATP-induced structural regulation of multistep DNA repair processes.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphatases / chemistry
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism
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Bacterial Proteins / chemistry
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism
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Base Pair Mismatch / genetics*
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Computer Simulation
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DNA Repair / genetics*
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DNA, Bacterial / chemistry*
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DNA, Bacterial / genetics*
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DNA, Bacterial / metabolism
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DNA-Binding Proteins*
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Escherichia coli Proteins*
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Genome, Bacterial*
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Models, Molecular
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MutS DNA Mismatch-Binding Protein
Substances
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Bacterial Proteins
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DNA, Bacterial
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DNA-Binding Proteins
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Escherichia coli Proteins
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Adenosine Triphosphatases
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MutS DNA Mismatch-Binding Protein
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MutS protein, E coli