f1样atp酶对支原体滑行运动的二聚体组装。

IF 12.5 1区 综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES
Science Advances Pub Date : 2025-02-28 Epub Date: 2025-02-26 DOI:10.1126/sciadv.adr9319
Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Tomoko Miyata, Keisuke Kawakami, Junso Fujita, Tasuku Hamaguchi, Keiichi Namba, Makoto Miyata
{"title":"f1样atp酶对支原体滑行运动的二聚体组装。","authors":"Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Tomoko Miyata, Keisuke Kawakami, Junso Fujita, Tasuku Hamaguchi, Keiichi Namba, Makoto Miyata","doi":"10.1126/sciadv.adr9319","DOIUrl":null,"url":null,"abstract":"<p><p>Rotary ATPases, including F<sub>1</sub>F<sub>O</sub>-, V<sub>1</sub>V<sub>O</sub>-, and A<sub>1</sub>A<sub>O</sub>-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, <i>Mycoplasma mobile</i>, a dimeric F<sub>1</sub>-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F<sub>1</sub>-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F<sub>1</sub>F<sub>O</sub>-ATPases. The F<sub>1</sub>-like ATPase unit associated by two subunits GliD and GliE was named G<sub>1</sub>-ATPase as an R<sub>1</sub> domain of rotary ATPases. G<sub>1</sub>-β subunit, a homolog of the F<sub>1</sub>-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F<sub>1</sub>-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G<sub>1</sub>-ATPase drives the <i>Mycoplasma</i> gliding motility.</p>","PeriodicalId":21609,"journal":{"name":"Science Advances","volume":"11 9","pages":"eadr9319"},"PeriodicalIF":12.5000,"publicationDate":"2025-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11864180/pdf/","citationCount":"0","resultStr":"{\"title\":\"Dimeric assembly of F<sub>1</sub>-like ATPase for the gliding motility of <i>Mycoplasma</i>.\",\"authors\":\"Takuma Toyonaga, Takayuki Kato, Akihiro Kawamoto, Tomoko Miyata, Keisuke Kawakami, Junso Fujita, Tasuku Hamaguchi, Keiichi Namba, Makoto Miyata\",\"doi\":\"10.1126/sciadv.adr9319\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Rotary ATPases, including F<sub>1</sub>F<sub>O</sub>-, V<sub>1</sub>V<sub>O</sub>-, and A<sub>1</sub>A<sub>O</sub>-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, <i>Mycoplasma mobile</i>, a dimeric F<sub>1</sub>-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F<sub>1</sub>-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F<sub>1</sub>F<sub>O</sub>-ATPases. The F<sub>1</sub>-like ATPase unit associated by two subunits GliD and GliE was named G<sub>1</sub>-ATPase as an R<sub>1</sub> domain of rotary ATPases. G<sub>1</sub>-β subunit, a homolog of the F<sub>1</sub>-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F<sub>1</sub>-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G<sub>1</sub>-ATPase drives the <i>Mycoplasma</i> gliding motility.</p>\",\"PeriodicalId\":21609,\"journal\":{\"name\":\"Science Advances\",\"volume\":\"11 9\",\"pages\":\"eadr9319\"},\"PeriodicalIF\":12.5000,\"publicationDate\":\"2025-02-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11864180/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Science Advances\",\"FirstCategoryId\":\"103\",\"ListUrlMain\":\"https://doi.org/10.1126/sciadv.adr9319\",\"RegionNum\":1,\"RegionCategory\":\"综合性期刊\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2025/2/26 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q1\",\"JCRName\":\"MULTIDISCIPLINARY SCIENCES\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science Advances","FirstCategoryId":"103","ListUrlMain":"https://doi.org/10.1126/sciadv.adr9319","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/2/26 0:00:00","PubModel":"Epub","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}
引用次数: 0

摘要

旋转atp酶,包括F1FO-, V1VO-和a1ao - atp酶,是分子马达,表现为能量转换的旋转运动。在移动支原体(Mycoplasma mobile)中,一种二聚体f1样atp酶在细胞内形成链状结构,被认为可以驱动滑动运动。然而,力的产生和传递机制仍不清楚。我们确定了二聚体f1样atp酶复合物的电子低温显微镜(cryo-EM)结构。该结构显示出与二聚体f1fo - atp酶不同的组装。由两个亚基GliD和GliE连接的f1样atp酶单元作为旋转atp酶的R1结构域被命名为g1 - atp酶。G1-β亚基是f1 - atp酶催化亚基的同系物,具有特异性的n端区域,该区域将糖酵解酶磷酸甘油酸激酶整合到复合物中。该ATPase的结构特征与F1-ATPase具有很强的相似性,表明其基于旋转催化机制的旋转。总的来说,低温电镜结构提供了对g1 - atp酶驱动支原体滑动运动的机制的见解。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Dimeric assembly of F1-like ATPase for the gliding motility of Mycoplasma.

Rotary ATPases, including F1FO-, V1VO-, and A1AO-ATPases, are molecular motors that exhibit rotational movements for energy conversion. In the gliding bacterium, Mycoplasma mobile, a dimeric F1-like ATPase forms a chain structure within the cell, which is proposed to drive the gliding motility. However, the mechanisms of force generation and transmission remain unclear. We determined the electron cryomicroscopy (cryo-EM) structure of the dimeric F1-like ATPase complex. The structure revealed an assembly distinct from those of dimeric F1FO-ATPases. The F1-like ATPase unit associated by two subunits GliD and GliE was named G1-ATPase as an R1 domain of rotary ATPases. G1-β subunit, a homolog of the F1-ATPase catalytic subunit, exhibited a specific N-terminal region that incorporates the glycolytic enzyme, phosphoglycerate kinase into the complex. Structural features of the ATPase displayed strong similarities to F1-ATPase, suggesting a rotation based on the rotary catalytic mechanism. Overall, the cryo-EM structure provides insights into the mechanism through which G1-ATPase drives the Mycoplasma gliding motility.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Science Advances
Science Advances 综合性期刊-综合性期刊
CiteScore
21.40
自引率
1.50%
发文量
1937
审稿时长
29 weeks
期刊介绍: Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信