3.88 Å structure of cytoplasmic polyhedrosis virus by cryo-electron microscopy

多面体 衣壳 核糖核酸 生物物理学 细胞质 低温电子显微 化学 结晶学 生物 细胞生物学 病毒 病毒学 生物化学 基因 重组DNA 夜蛾
作者
Xuekui Yu,Lei Jin,Zhen Zhou
出处
期刊:Nature [Springer Nature]
卷期号:453 (7193): 415-419 被引量:277
标识
DOI:10.1038/nature06893
摘要

Cytoplasmic polyhedrosis virus (CPV) is a member of a large family of double-stranded RNA viruses, but it is unique in having a single shell capsid yet being fully capable of cell entry and mRNA transcription. The structure of this virus has now been determined by single-particle cryo-electron microscopy (cryoEM) to a resolution of 3.88 Å. The technique allows the polypeptide backbone to be traced without the need to make a crystal. The high-resolution structure shows how conformational switching is exploited to make railroad-like 'sliding' tracks for RNA packing and transcription and reveals an mRNA releasing hole coupled with distinctive capping machinery. With this and several other recent publications, cryo-electron microscopy underlines its credentials as a system capable of atomic-resolution in structural studies. This paper presents a high resolution structure of the cytoplasmic polyhedroasis virus (CPV) obtained by single particle cryo electron microscopy, and shows that the polypeptide backbone can be traced without the need of making a crystal. Cytoplasmic polyhedrosis virus (CPV) is unique within the Reoviridae family in having a turreted single-layer capsid contained within polyhedrin inclusion bodies, yet being fully capable of cell entry and endogenous RNA transcription1,2,3,4. Biochemical data have shown that the amino-terminal 79 residues of the CPV turret protein (TP) is sufficient to bring CPV or engineered proteins into the polyhedrin matrix for micro-encapsulation5,6. Here we report the three-dimensional structure of CPV at 3.88 Å resolution using single-particle cryo-electron microscopy. Our map clearly shows the turns and deep grooves of α-helices, the strand separation in β-sheets, and densities for loops and many bulky side chains; thus permitting atomic model-building effort from cryo-electron microscopy maps. We observed a helix-to-β-hairpin conformational change between the two conformational states of the capsid shell protein in the region directly interacting with genomic RNA. We have also discovered a messenger RNA release hole coupled with the mRNA capping machinery unique to CPV. Furthermore, we have identified the polyhedrin-binding domain, a structure that has potential in nanobiotechnology applications.

科研通智能强力驱动
Strongly Powered by AbleSci AI
更新
大幅提高文件上传限制,最高150M (2024-4-1)

科研通是完全免费的文献互助平台,具备全网最快的应助速度,最高的求助完成率。 对每一个文献求助,科研通都将尽心尽力,给求助人一个满意的交代。
实时播报
优美的面包完成签到 ,获得积分10
刚刚
刚刚
aaa完成签到,获得积分20
1秒前
2秒前
一只小羊完成签到,获得积分20
2秒前
aaa发布了新的文献求助10
4秒前
277发布了新的文献求助10
5秒前
罗小黑完成签到 ,获得积分10
7秒前
无奈满天完成签到,获得积分10
8秒前
wayne完成签到,获得积分10
8秒前
9秒前
刘十九完成签到,获得积分10
9秒前
无名完成签到,获得积分10
9秒前
背后飞柏发布了新的文献求助10
9秒前
11秒前
11秒前
12秒前
最长的旅途完成签到,获得积分20
13秒前
追寻的冬寒完成签到 ,获得积分10
14秒前
15秒前
Maple发布了新的文献求助10
15秒前
15秒前
背后飞柏完成签到,获得积分20
16秒前
16秒前
123完成签到,获得积分10
17秒前
17秒前
JY完成签到,获得积分10
18秒前
HUI821526完成签到,获得积分10
18秒前
Liuyun发布了新的文献求助10
19秒前
大个应助卓疾采纳,获得10
20秒前
星辰大海应助aaa采纳,获得10
20秒前
21秒前
嗯嗯发布了新的文献求助10
21秒前
qrj发布了新的文献求助10
21秒前
22秒前
scq发布了新的文献求助10
22秒前
沉静的以珊完成签到,获得积分10
24秒前
大模型应助灵巧的白昼采纳,获得150
24秒前
思源应助灵巧的白昼采纳,获得10
24秒前
斯文败类应助灵巧的白昼采纳,获得10
24秒前
高分求助中
The ACS Guide to Scholarly Communication 2500
Sustainability in Tides Chemistry 2000
Pharmacogenomics: Applications to Patient Care, Third Edition 1000
Studien zur Ideengeschichte der Gesetzgebung 1000
TM 5-855-1(Fundamentals of protective design for conventional weapons) 1000
Threaded Harmony: A Sustainable Approach to Fashion 810
《粉体与多孔固体材料的吸附原理、方法及应用》(需要中文翻译版,化学工业出版社,陈建,周力,王奋英等译) 500
热门求助领域 (近24小时)
化学 医学 生物 材料科学 工程类 有机化学 生物化学 物理 内科学 纳米技术 计算机科学 化学工程 复合材料 基因 遗传学 催化作用 物理化学 免疫学 量子力学 细胞生物学
热门帖子
关注 科研通微信公众号,转发送积分 3083756
求助须知:如何正确求助?哪些是违规求助? 2737102
关于积分的说明 7543295
捐赠科研通 2386458
什么是DOI,文献DOI怎么找? 1265484
科研通“疑难数据库(出版商)”最低求助积分说明 613100
版权声明 597951