Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA
文献类型：期刊论文
| 作者 | Wei Y(魏勇); Zhang H(张衡) ; Gao ZQ(高增强); Wei, Y; Zhang, H; Gao, ZQ; Wang, WJ; Shtykova, EV; Xu, JH; Liu, QS
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| 刊名 | JOURNAL OF STRUCTURAL BIOLOGY
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| 出版日期 | 2012 |
| 卷号 | 179期号:1页码:29-40 |
| 关键词 | rRNA methyltransferase Dimeric conformation AdoMet binding domain Cytidine recognition domain Small-angle X-ray scattering Solution structure |
| 英文摘要 | RsmH is a specific AdoMet-dependent methyltransferase (MTase) responsible for N-4-methylation of C1402 in 16S rRNA and conserved in almost all species of bacteria. The methylcytidine interacts with the P-site codon of the mRNA and increases ribosomal decoding fidelity. In this study, high resolution crystal structure (2.25 angstrom) of Escherichia coil RsmH in complex with AdoMet and cytidine (the putative rRNA binding site) was determined. The structural analysis demonstrated that the complex consists of two distinct but structurally related domains: the typical MTase domain and the putative substrate recognition and binding domain. A deep pocket was found in the conserved AdoMet binding domain. It was also found that the cytidine bound far from AdoMet with the distance of 25.9 angstrom. It indicates that the complex is not in a catalytically active state, and structural rearrangement of RsmH or the nucleotides neighboring C1402 may be necessary to trigger catalysis. Although there is only one molecule in the asymmetric unit of the crystals, RsmH can form a compact dimer across a crystallographic twofold axis. Further analysis of RsmH by small-angle X-ray scattering (SAXS) also revealed the dimer in solution, but with a more flexible conformation than that in crystal, likely resulting from the absence of the substrate. It implies that an active status of RsmH in vivo is achieved by a formation of the dimeric architecture. In general, crystal and solution structural analysis provides new information on the mechanism of the methylation of the fine-tuning ribosomal decoding center by the RsmH. (C) 2012 Elsevier Inc. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics; Cell Biology |
| 收录类别 | SCI |
| WOS记录号 | WOS:000305775400004 |
| 公开日期 | 2016-05-03 |
| 源URL | [http://ir.ihep.ac.cn/handle/311005/223774]  |
| 专题 | 高能物理研究所_多学科研究中心 |
| 推荐引用方式 GB/T 7714 | Wei Y,Zhang H,Gao ZQ,et al. Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA[J]. JOURNAL OF STRUCTURAL BIOLOGY,2012,179(1):29-40. |
| APA | 魏勇.,张衡.,高增强.,Wei, Y.,Zhang, H.,...&董宇辉.(2012).Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA.JOURNAL OF STRUCTURAL BIOLOGY,179(1),29-40. |
| MLA | 魏勇,et al."Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA".JOURNAL OF STRUCTURAL BIOLOGY 179.1(2012):29-40. |
入库方式： OAI收割
来源：高能物理研究所
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