Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI
文献类型：期刊论文
| 作者 | Dong, YH; Zhang, LB; Zhang, H; Liu, GF; Wang, L; Wang, J; Gao, ZQ; Gong, Y; Zhao MH(赵默涵); Zhang H(张衡)
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| 刊名 | PLOS ONE
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| 出版日期 | 2016 |
| 卷号 | 11期号:10 |
| DOI | 10.1371/journal.pone.0163816 |
| 通讯作者 | 龚勇 |
| 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. |
| 语种 | 英语 |
| WOS记录号 | WOS:000385697600042 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/260492]  |
| 专题 | 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 |
| 推荐引用方式 GB/T 7714 | Dong, YH,Zhang, LB,Zhang, H,et al. Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI[J]. PLOS ONE,2016,11(10). |
| APA | Dong, YH.,Zhang, LB.,Zhang, H.,Liu, GF.,Wang, L.,...&Zhao, MH.(2016).Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI.PLOS ONE,11(10). |
| MLA | Dong, YH,et al."Structural Insights into the Methylation of C1402 in 16S rRNA by Methyltransferase RsmI".PLOS ONE 11.10(2016). |
入库方式： OAI收割
来源：高能物理研究所
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