Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates.

@article{Natrajan2003StructuresOE,
  title={Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates.},
  author={Ganesh Natrajan and Meindert Hugo Lamers and Jacqueline H. Enzlin and Herrie H. K. Winterwerp and Anastassis Perrakis and Titia Sixma},
  journal={Nucleic acids research},
  year={2003},
  volume={31 16},
  pages={4814-21}
}
We have refined a series of isomorphous crystal structures of the Escherichia coli DNA mismatch repair enzyme MutS in complex with G:T, A:A, C:A and G:G mismatches and also with a single unpaired thymidine. In all these structures, the DNA is kinked by approximately 60 degrees upon protein binding. Two residues widely conserved in the MutS family are involved in mismatch recognition. The phenylalanine, Phe 36, is seen stacking on one of the mismatched bases. The same base is also seen forming a… CONTINUE READING