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

被引：123

作者：

Natrajan, G ^{[1
]}

Lamers, MH ^{[1
]}

Enzlin, JH ^{[1
]}

Winterwerp, HHK ^{[1
]}

Perrakis, A ^{[1
]}

Sixma, TK ^{[1
]}

机构：

[1] Netherlands Canc Inst, Div Mol Carcinogenesis, NL-1066 CX Amsterdam, Netherlands

来源：

NUCLEIC ACIDS RESEARCH | 2003年 / 31卷 / 16期

关键词：

D O I：

10.1093/nar/gkg677

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 similar to60degrees 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.

引用

页码：4814 / 4821

页数：8

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