Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI
Zhao MH(赵默涵); Zhang H(张衡); Gao ZQ(高增强); Dong YH(董宇辉); Gong Y(龚勇); Zhao, MH; Zhang, H; Liu, GF; Wang, L; Wang, J; Gao, ZQ; Dong, YH; Zhang, LB; Gong, Y
刊名PLOS ONE
2016
卷号11期号:10
DOI10.1371/journal.pone.0163816
通讯作者龚勇
文章类型期刊论文
英文摘要RsmI and RsmH are conserved S-Adenosylmethionine (AdoMet)-dependent methyltransferases (MTases) that are responsible for the 2'-O-methylation and N-4-methylation of C1402 in bacterial 16S rRNA, respectively. Methylation of m(4)Cm1402 plays a role in fine-tuning the shape and functions of the P-site to increase the decoding fidelity, and was recently found to contribute to the virulence of Staphylococcus aureus in host animals. Here we report the 2.20-angstrom crystal structure of homodimeric RsmI from Escherichia coli in complex with the cofactor AdoMet. RsmI consists of an N-terminal putative RNA-binding domain (NTD) and a C-terminal catalytic domain (CTD) with a Rossmann-like fold, and belongs to the class III MTase family. AdoMet is specifically bound into a negatively charged deep pocket formed by both domains by making extensive contacts. Structure-based mutagenesis and isothermal titration calorimetry (ITC) assays revealed Asp100 and Ala124 are vital for AdoMet-binding. Although the overall fold of RsmI shows remarkable similarities to the characterized MTases involved in vitamin B12 biosynthesis, it exhibits a distinct charge distribution especially around the AdoMet-binding pocket because of different substrate specificity. The docking model of RsmI-AdoMet-RNA ternary complex suggested a possible base-flipping mechanism of the substrate RNA that has been observed in several known RNA MTases. Our structural and biochemical studies provide novel insights into the catalytic mechanism of C1402 methylation in 16S rRNA.
类目[WOS]Multidisciplinary Sciences
关键词[WOS]ESCHERICHIA-COLI ; CRYSTAL ; ENZYME
语种英语
WOS记录号WOS:000385697600042
引用统计
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/260492
专题中国科学院高能物理研究所_多学科研究中心_期刊论文
中国科学院高能物理研究所_多学科研究中心
作者单位中国科学院高能物理研究所
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GB/T 7714
Zhao MH,Zhang H,Gao ZQ,et al. Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI[J]. PLOS ONE,2016,11(10).
APA 赵默涵.,张衡.,高增强.,董宇辉.,龚勇.,...&Gong, Y.(2016).Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI.PLOS ONE,11(10).
MLA 赵默涵,et al."Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI".PLOS ONE 11.10(2016).
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