Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates
| Autor: | Meindert H. Lamers, Titia K. Sixma, Ganesh Natrajan, Jacqueline H. Enzlin, Herrie H.K. Winterwerp, Anastassis Perrakis |
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| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular congenital hereditary and neonatal diseases and abnormalities MutS DNA Mismatch-Binding Protein Stereochemistry Base Pair Mismatch Protein Conformation Phenylalanine Glutamic Acid Biology Substrate Specificity chemistry.chemical_compound Protein structure Bacterial Proteins MutS-1 Genetics Escherichia coli Binding site Adenosine Triphosphatases Binding Sites Escherichia coli Proteins Hydrogen Bonding DNA Articles Thymine Protein Structure Tertiary DNA-Binding Proteins chemistry Biochemistry DNA mismatch repair |
| Zdroj: | Nucleic acids research. 31(16) |
| ISSN: | 1362-4962 |
| Popis: | 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 hydrogen bond to the glutamate Glu 38. This hydrogen bond involves the N7 if the base stacking on Phe 36 is a purine and the N3 if it is a pyrimidine (thymine). Thus, MutS uses a common binding mode to recognize a wide range of mismatches. |
| Databáze: | OpenAIRE |
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