Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 A resolution

Su Zhaoming; Zhang Kaiming; Kappel Kalli; Li Shanshan; Palo Michael Z.; Pintilie Grigore D.; Rangan Ramya; Luo Bingnan; Wei Yuquan; Das Rhiju; Chiu Wah

首页> 外文期刊>Nature >Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 A resolution

【24h】

Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 A resolution

机译：3.1分辨率的全长四晶烯核酶的Cryo-EM结构

获取原文

获取原文并翻译 | 示例

掌桥外文数据库（机构版） >>

开具论文收录证明 >>

文献代查 >>

页面导航

摘要
著录项
相似文献
相关主题

摘要

Single-particle cryogenic electron microscopy (cryo-EM) has become a standard technique for determining protein structures at atomic resolution(1-3). However, cryo-EM studies of protein-free RNA are in their early days. The Tetrahymena thermophila group I self-splicing intron was the first ribozyme to be discovered and has been a prominent model system for the study of RNA catalysis and structure-function relationships(4), but its full structure remains unknown. Here we report cryo-EM structures of the full-length Tetrahymena ribozyme in substrate-free and bound states at a resolution of 3.1 angstrom. Newly resolved peripheral regions form two coaxially stacked helices; these are interconnected by two kissing loop pseudoknots that wrap around the catalytic core and include two previously unforeseen (to our knowledge) tertiary interactions. The global architecture is nearly identical in both states; only the internal guide sequence and guanosine binding site undergo a large conformational change and a localized shift, respectively, upon binding of RNA substrates. These results provide a long-sought structural view of a paradigmatic RNA enzyme and signal a new era for the cryo-EM-based study of structure-function relationships in ribozymes.

机译：单颗粒低温电子显微镜（Cryo-EM）已成为用于确定原子分辨率（1-3）以确定蛋白质结构的标准技术（1-3）。然而，在早期的蛋白质RNA的Cryo-EM研究是早期的。 Tetrahymena Thermophila群I自拼接内含子是第一个发现的核酶，并且已经是研究RNA催化和结构功能关系（4）的突出模型系统，但其全结构仍然未知。在这里，我们以3.1埃的分辨率在无基质和结合状态下报告全长Tetrahymena核酶的冷冻EM结构。新分离的外围区域形成两个同轴堆叠的螺旋;这些通过两个接吻环伪通孔互连，其缠绕在催化核心周围，并包括先前未预见的（对我们的知识）三级相互作用。全球架构在两个州几乎相同;在RNA基材结合后，仅内部导向序列和鸟苷结合位点分别经历大的构象变化和局部偏移。这些结果提供了一种广视RNA酶的长寻求结构图，并以核酶中的基于Cryo-em的基于结构关系的研究发出新的时代。

著录项

来源
《Nature》 |2021年第7873期|603-607|共5页
作者
Su Zhaoming; Zhang Kaiming; Kappel Kalli; Li Shanshan; Palo Michael Z.; Pintilie Grigore D.; Rangan Ramya; Luo Bingnan; Wei Yuquan; Das Rhiju; Chiu Wah;
展开▼
作者单位

Sichuan Univ State Key Lab Biotherapy Chengdu Peoples R China|Sichuan Univ Canc Ctr Dept Geriatr Chengdu Peoples R China|Sichuan Univ Natl Clin Res Ctr Geriatr West China Hosp Chengdu Peoples R China|Stanford Univ Dept Bioengn Stanford CA 94305 USA|Stanford Univ James H Clark Ctr Stanford CA 94305 USA;

Stanford Univ Dept Bioengn Stanford CA 94305 USA|Stanford Univ James H Clark Ctr Stanford CA 94305 USA|Univ Sci & Technol China Hefei Natl Lab Phys Sci Microscale MOE Key Lab Membraneless Organelles & Cellular Dy Hefei Peoples R China|Univ Sci & Technol China Sch Life Sci Hefei Peoples R China;

Stanford Univ Biophys Program Stanford CA 94305 USA;

Stanford Univ Dept Bioengn Stanford CA 94305 USA|Stanford Univ James H Clark Ctr Stanford CA 94305 USA|Univ Sci & Technol China Hefei Natl Lab Phys Sci Microscale MOE Key Lab Membraneless Organelles & Cellular Dy Hefei Peoples R China|Univ Sci & Technol China Sch Life Sci Hefei Peoples R China;

Stanford Univ Biophys Program Stanford CA 94305 USA;

Stanford Univ Dept Bioengn Stanford CA 94305 USA|Stanford Univ James H Clark Ctr Stanford CA 94305 USA;

Stanford Univ Biophys Program Stanford CA 94305 USA;

Sichuan Univ State Key Lab Biotherapy Chengdu Peoples R China|Sichuan Univ Canc Ctr Dept Geriatr Chengdu Peoples R China|Sichuan Univ Natl Clin Res Ctr Geriatr West China Hosp Chengdu Peoples R China;

Sichuan Univ State Key Lab Biotherapy Chengdu Peoples R China|Sichuan Univ Canc Ctr Dept Geriatr Chengdu Peoples R China|Sichuan Univ Natl Clin Res Ctr Geriatr West China Hosp Chengdu Peoples R China;

Stanford Univ Biophys Program Stanford CA 94305 USA|Stanford Univ Dept Biochem Stanford CA 94305 USA|Stanford Univ Dept Phys Stanford CA 94305 USA;

Stanford Univ Dept Bioengn Stanford CA 94305 USA|Stanford Univ James H Clark Ctr Stanford CA 94305 USA|SLAC Natl Accelerator Lab SSRL Div CryoEM & Bioimaging Menlo Pk CA 94025 USA;

展开▼
收录信息美国《科学引文索引》(SCI);美国《工程索引》(EI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
原文格式 PDF
正文语种 eng
中图分类
关键词

相似文献

外文文献
中文文献
专利

1. Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 angstrom Resolution [J] . Sevvana Madhumati, Long Feng, Miller Andrew S., Structure . 2018,第9期

机译：3.1 Angstrom分辨率的成熟Zika病毒Cryo-EM结构的改进与分析
2. Cryo-EM structures of apo and antagonist-bound human Ca_v3.1 [J] . Zhao Yanyu, Huang Gaoxingyu, Wu Qiurong, Nature . 2019,第7787期

机译：载脂蛋白和结合拮抗剂的人类Ca_v3.1的低温电磁结构
3. Cryo-EM structure of a herpesvirus capsid at 3.1 A [J] . Yuan Shuai, Wang Jialing, Zhu Dongjie, Science . 2018,第6384期

机译：疱疹病毒衣壳在3.1 A时的低温电磁结构
4. A Pattern Recognition Tool for Medium-Resolution Cryo-EM Density Maps and Low-Resolution Cryo-ET Density Maps [C] . Devin Haslam, Salim Sazzed, Willy Wriggers, International symposium on bioinformatics research and applications . 2018

机译：中分辨率Cryo-EM密度图和低分辨率Cryo-ET密度图的模式识别工具
5. Exploration of Schistosoma mansoni hammerhead ribozyme catalysis and structure: Towards direct observation of cleavage and ligation, and a 1.55 Å full-length magnesium ion (II)-bound crystal structure [D] . Anderson, Michael Harrison 2012

机译：曼氏血吸虫锤头状核酶催化和结构的探索：直接观察裂解和连接，以及1.55Å全长镁离子（II）结合的晶体结构
6. Refinement and Analysis of the Mature Zika Virus Cryo-EM Structure at 3.1 Å Resolution [O] . Madhumati Sevvana, Feng Long, Andrew S. Miller, -1

机译：分辨率为3.1Å的成熟寨卡病毒Cryo-EM结构的细化和分析
7. Cryo-EM structure of the MinCD copolymeric filament from Pseudomonas aeruginosa at 3.1 Å resolution [O] . Andrzej Szewczak-Harris, James Wagstaff, Jan Löwe 2019

机译：Pseudomonas Aeruginosa的MinCD共聚丝的Cryo-EM结构在3.1Å分辨率下

Cryo-EM structures of full-length Tetrahymena ribozyme at 3.1 A resolution

摘要

著录项

相似文献

相关主题

期刊订阅