IHEP OpenIR  > 多学科研究中心
Crystal and solution structures of methyltransferase RsmH provide basis for methylation of C1402 in 16S rRNA
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; Dong, YH; Wang WJ(王文佳); Xu JH(徐建华); Liu QS(刘全胜); Dong YH(董宇辉)
2012
发表期刊JOURNAL OF STRUCTURAL BIOLOGY
卷号179期号:1页码:29-40
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.
关键词rRNA methyltransferase Dimeric conformation AdoMet binding domain Cytidine recognition domain Small-angle X-ray scattering Solution structure
学科领域Biochemistry & Molecular Biology; Biophysics; Cell Biology
DOI10.1016/j.jsb.2012.04.011
收录类别SCI
WOS记录号WOS:000305775400004
引用统计
被引频次:8[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://ir.ihep.ac.cn/handle/311005/223774
专题多学科研究中心
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.
条目包含的文件
文件名称/大小 文献类型 版本类型 开放类型 使用许可
390.pdf(3772KB)期刊论文作者接受稿限制开放CC BY-NC-SA请求全文
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[魏勇]的文章
[张衡]的文章
[高增强]的文章
百度学术
百度学术中相似的文章
[魏勇]的文章
[张衡]的文章
[高增强]的文章
必应学术
必应学术中相似的文章
[魏勇]的文章
[张衡]的文章
[高增强]的文章
相关权益政策
暂无数据
收藏/分享
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。