PMID:11048710
| Citation |
Obmolova, G, Ban, C, Hsieh, P and Yang, W (2000) Crystal structures of mismatch repair protein MutS and its complex with a substrate DNA. Nature 407:703-10 |
|---|---|
| Abstract |
DNA mismatch repair is critical for increasing replication fidelity in organisms ranging from bacteria to humans. MutS protein, a member of the ABC ATPase superfamily, recognizes mispaired and unpaired bases in duplex DNA and initiates mismatch repair. Mutations in human MutS genes cause a predisposition to hereditary nonpolyposis colorectal cancer as well as sporadic tumours. Here we report the crystal structures of a MutS protein and a complex of MutS with a heteroduplex DNA containing an unpaired base. The structures reveal the general architecture of members of the MutS family, an induced-fit mechanism of recognition between four domains of a MutS dimer and a heteroduplex kinked at the mismatch, a composite ATPase active site composed of residues from both MutS subunits, and a transmitter region connecting the mismatch-binding and ATPase domains. The crystal structures also provide a molecular framework for understanding hereditary nonpolyposis colorectal cancer mutations and for postulating testable roles of MutS. |
| Links |
PubMed Online version:10.1038/35037509 |
| Keywords |
Adenosine Triphosphatases/metabolism; Adenosine Triphosphate/metabolism; Amino Acid Sequence; Bacterial Proteins/chemistry; Bacterial Proteins/metabolism; Base Pair Mismatch; Binding Sites; Crystallography, X-Ray; DNA Repair; DNA, Bacterial/chemistry; DNA, Bacterial/metabolism; DNA-Binding Proteins/chemistry; DNA-Binding Proteins/metabolism; Escherichia coli Proteins; Macromolecular Substances; Models, Biological; Models, Molecular; Molecular Sequence Data; MutS DNA Mismatch-Binding Protein; Nucleic Acid Conformation; Nucleic Acid Heteroduplexes; Protein Binding; Protein Conformation; Thermus/genetics |
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