The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate

Foster PG.; Nunes CR.; Greene P.; Moustakas D.; Stroud RM.

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The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate

机译：RNA m（5）C甲基转移酶Fmu的第一个结构可洞悉RNA底物的催化机制和特异性结合

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The crystal structure of E. coli Fmu, determined at 1.65 Angstrom resolution for the apoenzyme and 2.1 Angstrom resolution in complex with Ado Met, is the first representative of the 5-methylcytosine RNA methyltransferase family that includes the human nucleolar proliferation-associated protein p120. Fmu contains three subdomains which share structural homology to DNA m(5)C methyl-transferases and two RNA binding protein families. In the binary complex, the AdoMet cofactor is positioned within the active site near a novel arrangement of two conserved cysteines that function in cytosine methylation. The site is surrounded by a positively charged cleft large enough to bind its unique target stem loop within 16S rRNA. Docking of this stem loop RNA into the structure followed by molecular mechanics shows that the Fmu structure is consistent with binding to the folded RNA substrate. [References: 37]

机译：大肠杆菌Fmu的晶体结构是脱辅酶的分辨率为1.65埃，与Ado Met的复合物的分辨率为2.1埃，是包括人核仁增殖相关蛋白p120在内的5-甲基胞嘧啶RNA甲基转移酶家族的第一个代表。 Fmu包含三个亚结构域，与DNA m（5）C甲基转移酶和两个RNA结合蛋白家族具有相同的结构同源性。在二元复合物中，AdoMet辅因子位于活性位点附近，在两个保守的半胱氨酸的新排列中起作用，它们在胞嘧啶甲基化中起作用。该位点被带正电荷的裂口围绕，其大小足以结合其在16S rRNA中的独特靶标茎环。将该茎环RNA对接到结构中，然后进行分子力学分析，表明Fmu结构与结合到折叠的RNA底物上是一致的。 [参考：37]

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《Structure》 |2003年第12期|共12页
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Foster PG.; Nunes CR.; Greene P.; Moustakas D.; Stroud RM.;
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正文语种 eng
中图分类生物科学;
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16s ribosomal-rna; Crystal-structure; Dna methyltransferase; Angstrom resolution; Escherichia-coli; Molecular-dynamics; Cysteine residues; Methylation; Identification; Complexes;

机译：16s核糖体-rna;晶体结构;Dna甲基转移酶;埃分辨;大肠埃希菌;分子动力学;半胱氨酸残基;甲基化;鉴定;复合物;

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1. The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate [J] . Foster PG., Nunes CR., Greene P., Structure . 2003,第12期

机译：RNA m（5）C甲基转移酶Fmu的第一个结构可洞悉RNA底物的催化机制和特异性结合
2. Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate. [J] . Shao Z, Yan W, Peng J, Nucleic Acids Research . 2014,第1期

机译：TRNA M1G9甲基转移酶TRM10的晶体结构：洞察催化机理和TRNA基材的识别。
3. Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate [J] . Deshun Gong, Fudong Li, Jihui Wu, Nucleic acids research . 2014,第1期

机译：tRNA m1G9甲基转移酶Trm10的晶体结构：深入了解tRNA底物的催化机制和识别
4. Broad substrate RNA specificity of Trm1 (tRNA (m22G26) methyltransferase) from Aquifex aeolicus [C] . Awai Takako, Hori Hiroyuki International Symposium on Micro-NanoMechatronics and Human Science . 2008

机译：来自Aquifex Aeolicus的宽基板RNA特异性TRM1（TRNA（TRNA（m 2
5. Mutations within the second coordination sphere of catalytic iron (II) in human phenylalanine hydroxylase (hPAH) that affect the environment and electronic geometry of iron (II) are implicated in its mechanism, substrate binding and specificity. [D] . Daoud Kinzie, Sylvia Munir. 2005

机译：人类苯丙氨酸羟化酶（hPAH）中催化铁（II）的第二个配位域内的突变会影响铁（II）的环境和电子几何结构，其机制，底物结合和特异性都与它有关。
6. Crystal structure of tRNA m1G9 methyltransferase Trm10: insight into the catalytic mechanism and recognition of tRNA substrate [O] . Zhenhua Shao, Wei Yan, Junhui Peng, 2014

机译：tRNA m1G9甲基转移酶Trm10的晶体结构：深入了解tRNA底物的催化机制和识别
7. The First Structure of an RNA m5C Methyltransferase, Fmu, Provides Insight into Catalytic Mechanism and Specific Binding of RNA Substrate [O] . Foster Paul G, Nunes Christa R, Greene Patricia, 2003

机译：RNA m5C甲基转移酶的第一个结构Fmu提供了对RNA底物的催化机理和特异性结合的深入了解

The first structure of an RNA m(5)C methyltransferase, Fmu, provides insight into catalytic mechanism and specific binding of RNA substrate

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