大肠杆菌DNA错配修复酶MutS与不同错配形成复合物的结构：多种底物的共同识别模式。
Structures of Escherichia coli DNA mismatch repair enzyme MutS in complex with different mismatches: a common recognition mode for diverse substrates.
作者信息
Natrajan Ganesh, Lamers Meindert H, Enzlin Jacqueline H, Winterwerp Herrie H K, Perrakis Anastassis, Sixma Titia K
机构信息
Division of Molecular Carcinogenesis, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX, Amsterdam, The Netherlands.
出版信息
Nucleic Acids Res. 2003 Aug 15;31(16):4814-21. doi: 10.1093/nar/gkg677.
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.
摘要
我们已优化了一系列大肠杆菌DNA错配修复酶MutS与G:T、A:A、C:A和G:G错配以及单个未配对胸腺嘧啶形成复合物的同晶型晶体结构。在所有这些结构中，DNA在蛋白质结合时会发生约60度的弯曲。MutS家族中两个广泛保守的残基参与错配识别。苯丙氨酸（Phe 36）堆积在其中一个错配碱基上。同一个碱基还与谷氨酸（Glu 38）形成氢键。如果堆积在Phe 36上的碱基是嘌呤，该氢键涉及N7；如果是嘧啶（胸腺嘧啶），则涉及N3。因此，MutS使用一种共同的结合模式来识别多种错配。
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