1oh5: Difference between revisions
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Revision as of 16:49, 30 October 2007
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THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH
OverviewOverview
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.
About this StructureAbout this Structure
1OH5 is a [Protein complex] structure of sequences from [Escherichia coli] with MG and ADP as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates., Natrajan G, Lamers MH, Enzlin JH, Winterwerp HH, Perrakis A, Sixma TK, Nucleic Acids Res. 2003 Aug 15;31(16):4814-21. PMID:12907723
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