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首页> 美国卫生研究院文献>The EMBO Journal >Crystal structure of a repair enzyme of oxidatively damaged DNA MutM (Fpg) from an extreme thermophile Thermus thermophilus HB8
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Crystal structure of a repair enzyme of oxidatively damaged DNA MutM (Fpg) from an extreme thermophile Thermus thermophilus HB8

机译：极端嗜热菌Thermus thermophilus HB8被氧化破坏的DNA MutM（Fpg）修复酶的晶体结构

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摘要

The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a trifunctional DNA base excision repair enzyme that removes a wide range of oxidatively damaged bases (N-glycosylase activity) and cleaves both the 3′- and 5′-phosphodiester bonds of the resulting apurinic/apyrimidinic site (AP lyase activity). The crystal structure of MutM from an extreme thermophile, Thermus thermophilus HB8, was determined at 1.9 Å resolution with multiwavelength anomalous diffraction phasing using the intrinsic Zn2+ ion of the zinc finger. MutM is composed of two distinct and novel domains connected by a flexible hinge. There is a large, electrostatically positive cleft lined by highly conserved residues between the domains. On the basis of the three-dimensional structure and taking account of previous biochemical experiments, we propose a DNA-binding mode and reaction mechanism for MutM. The locations of the putative catalytic residues and the two DNA-binding motifs (the zinc finger and the helix–two-turns–helix motifs) suggest that the oxidized base is flipped out from double-stranded DNA in the binding mode and excised by a catalytic mechanism similar to that of bifunctional base excision repair enzymes.
机译：MutM [甲酰胺基嘧啶DNA糖基化酶（Fpg）]蛋白是一种三功能DNA碱基切除修复酶，可去除各种氧化损伤的碱基（N-糖基化酶活性），并裂解所得产物的3'-和5'-磷酸二酯键嘌呤/无嘧啶位点（AP裂解酶活性）。使用锌指的本征Zn 2 + 离子通过多波长异常衍射定相，以1.9Å分辨率确定了来自极端嗜热菌嗜热栖热菌HB8的MutM的晶体结构。 MutM由通过柔性铰链连接的两个不同且新颖的域组成。在区域之间有一个大的，静电阳性的裂口，上面有高度保守的残基。在三维结构的基础上，考虑到以前的生化实验，我们提出了MutM的DNA结合模式和反应机理。假定的催化残基和两个DNA结合基序（锌指和螺旋-两圈-螺旋基序）的位置表明，氧化的碱基以结合方式从双链DNA中翻转出来，并被一个催化机制类似于双功能碱基切除修复酶。

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