Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme
Structure-Function Analysis of Escherichia coli MnmG (GidA), a Highly Conserved tRNA-Modifying Enzyme
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DOI：
10.1128/jb.00650-09
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发表时间：
2009-12-15
影响因子：
3.2
通讯作者：
Cygler, Miroslaw
中科院分区：
文献类型：
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作者：
Shi, Rong;Villarroya, Magda;Cygler, Miroslaw
MnmE-MnmG复合物参与tRNA修饰。我们已经确定了大肠杆菌MnmG在2.4埃分辨率的晶体结构，突变的高度保守的残基与黄素腺嘌呤二核苷酸（FAD）或tRNA结合和MnmE相互作用的推定作用，并分析了这些突变在体内和体外的影响。MnmG的有限胰蛋白酶解表明FAD结合后的显著构象变化。
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-angstrom resolution, mutated highly conserved residues with putative roles in flavin adenine dinucleotide (FAD) or tRNA binding and MnmE interaction, and analyzed the effects of these mutations in vivo and in vitro. Limited trypsinolysis of MnmG suggests significant conformational changes upon FAD binding.