1OH5

THE CRYSTAL STRUCTURE OF E. COLI MUTS BINDING TO DNA WITH A C:A MISMATCH

Summary for 1OH5

• Entry DOI: 10.2210/pdb1oh5/pdb
• Related: 1E3M 1NG9 1OH6 1OH7 1OH8
• Descriptor: DNA MISMATCH REPAIR PROTEIN MUTS, 5'-D(*AP*GP*CP*TP*GP*CP*CP*AP*CP*GP *CP*AP*CP*CP*AP*GP*TP*GP*TP*CP*AP*GP*CP*GP*TP *CP*CP*TP*AP*T)-3', 5'-D(*AP*TP*AP*GP*GP*AP*CP*GP*CP*TP *GP*AP*CP*AP*CP*TP*GP*GP*TP*GP*CP*AP*TP*GP*GP *CP*AP*GP*CP*T)-3', ... (6 entities in total)
• Functional Keywords: dna binding, mismatch recognition
• Biological source: ESCHERICHIA COLI; More
• Total number of polymer chains: 4
• Total formula weight: 198094.08

Authors

Natrajan, G.,Lamers, M.H.,Enzlin, J.H.,Winterwerp, H.H.K.,Perrakis, A.,Sixma, T.K. (deposition date: 2003-05-23, release date: 2003-08-08, Last modification date: 2023-12-13)

Primary citation

Natrajan, G.,Lamers, M.H.,Enzlin, J.H.,Winterwerp, H.H.K.,Perrakis, A.,Sixma, T.K.
Structures of E. Coli DNA Mismatch Repair Enzyme Muts in Complex with Different Mismatches: A Common Recognition Mode for Diverse Substrates
Nucleic Acids Res., 31:4814-, 2003

PubMed Abstract: 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.

PubMed: 12907723
DOI: 10.1093/NAR/GKG677

Experimental method

X-RAY DIFFRACTION (2.9 Å)