大肠杆菌MnmG（GidA）的结构-功能分析，一种高度保守的tRNA修饰酶。
Structure-function analysis of Escherichia coli MnmG (GidA), a highly conserved tRNA-modifying enzyme.
作者信息
Shi Rong, Villarroya Magda, Ruiz-Partida Rafael, Li Yunge, Proteau Ariane, Prado Silvia, Moukadiri Ismaïl, Benítez-Páez Alfonso, Lomas Rodrigo, Wagner John, Matte Allan, Velázquez-Campoy Adrián, Armengod M-Eugenia, Cygler Miroslaw
机构信息
Department of Biochemistry, McGill University, Montreal, Quebec, Canada.
出版信息
J Bacteriol. 2009 Dec;191(24):7614-9. doi: 10.1128/JB.00650-09. Epub 2009 Oct 2.
Abstract
The MnmE-MnmG complex is involved in tRNA modification. We have determined the crystal structure of Escherichia coli MnmG at 2.4-A 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.
摘要
MnmE-MnmG复合物参与tRNA修饰。我们已确定大肠杆菌MnmG在2.4埃分辨率下的晶体结构，对在黄素腺嘌呤二核苷酸（FAD）或tRNA结合以及MnmE相互作用中具有假定作用的高度保守残基进行了突变，并分析了这些突变在体内和体外的影响。对MnmG进行的有限胰蛋白酶消化表明，FAD结合后会发生显著的构象变化。
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Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate.保守的tRNA修饰酶GidA的晶体结构：对其与MnmE及底物相互作用的启示
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The GTPase activity and C-terminal cysteine of the Escherichia coli MnmE protein are essential for its tRNA modifying function.大肠杆菌MnmE蛋白的GTP酶活性和C端半胱氨酸对其tRNA修饰功能至关重要。
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