旋转式atp酶:型号、机器部件及技术规格。

Bioarchitecture Pub Date : 2013-01-01 DOI:10.4161/bioa.23301
Alastair G Stewart, Meghna Sobti, Richard P Harvey, Daniela Stock
{"title":"旋转式atp酶:型号、机器部件及技术规格。","authors":"Alastair G Stewart,&nbsp;Meghna Sobti,&nbsp;Richard P Harvey,&nbsp;Daniela Stock","doi":"10.4161/bioa.23301","DOIUrl":null,"url":null,"abstract":"<p><p>Rotary ATPases are molecular rotary motors involved in biological energy conversion. They either synthesize or hydrolyze the universal biological energy carrier adenosine triphosphate. Recent work has elucidated the general architecture and subunit compositions of all three sub-types of rotary ATPases. Composite models of the intact F-, V- and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual subunits or sub-complexes into low-resolution electron densities of the intact enzymes derived from electron cryo-microscopy. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria and mass-spectrometry has started to identify specifically bound lipids presumed to be essential for function. Taken together these molecular snapshots show that nano-scale rotary engines have much in common with basic design principles of man made machines from the function of individual \"machine elements\" to the requirement of the right \"fuel\" and \"oil\" for different types of motors.</p>","PeriodicalId":89329,"journal":{"name":"Bioarchitecture","volume":"3 1","pages":"2-12"},"PeriodicalIF":0.0000,"publicationDate":"2013-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.4161/bioa.23301","citationCount":"24","resultStr":"{\"title\":\"Rotary ATPases: models, machine elements and technical specifications.\",\"authors\":\"Alastair G Stewart,&nbsp;Meghna Sobti,&nbsp;Richard P Harvey,&nbsp;Daniela Stock\",\"doi\":\"10.4161/bioa.23301\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Rotary ATPases are molecular rotary motors involved in biological energy conversion. They either synthesize or hydrolyze the universal biological energy carrier adenosine triphosphate. Recent work has elucidated the general architecture and subunit compositions of all three sub-types of rotary ATPases. Composite models of the intact F-, V- and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual subunits or sub-complexes into low-resolution electron densities of the intact enzymes derived from electron cryo-microscopy. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria and mass-spectrometry has started to identify specifically bound lipids presumed to be essential for function. Taken together these molecular snapshots show that nano-scale rotary engines have much in common with basic design principles of man made machines from the function of individual \\\"machine elements\\\" to the requirement of the right \\\"fuel\\\" and \\\"oil\\\" for different types of motors.</p>\",\"PeriodicalId\":89329,\"journal\":{\"name\":\"Bioarchitecture\",\"volume\":\"3 1\",\"pages\":\"2-12\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2013-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.4161/bioa.23301\",\"citationCount\":\"24\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Bioarchitecture\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.4161/bioa.23301\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Bioarchitecture","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.4161/bioa.23301","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 24

摘要

旋转atp酶是参与生物能量转换的分子旋转马达。它们合成或水解通用的生物能量载体三磷酸腺苷。最近的工作已经阐明了所有三种旋转atp酶亚型的一般结构和亚基组成。通过将单个亚基或亚配合物的高分辨率x射线结构拟合到电子冷冻显微镜获得的完整酶的低分辨率电子密度中,构建了完整的F型,V型和a型atp酶的复合模型。电子冷冻断层扫描为真核生物线粒体内ATP合酶的超分子排列提供了新的见解,质谱法已经开始识别被认为对功能至关重要的特异性结合脂质。综上所述,这些分子快照表明,纳米级旋转发动机与人造机器的基本设计原则有很多共同之处,从单个“机器元件”的功能到不同类型的发动机对正确“燃料”和“油”的要求。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Rotary ATPases: models, machine elements and technical specifications.

Rotary ATPases: models, machine elements and technical specifications.

Rotary ATPases: models, machine elements and technical specifications.

Rotary ATPases: models, machine elements and technical specifications.

Rotary ATPases are molecular rotary motors involved in biological energy conversion. They either synthesize or hydrolyze the universal biological energy carrier adenosine triphosphate. Recent work has elucidated the general architecture and subunit compositions of all three sub-types of rotary ATPases. Composite models of the intact F-, V- and A-type ATPases have been constructed by fitting high-resolution X-ray structures of individual subunits or sub-complexes into low-resolution electron densities of the intact enzymes derived from electron cryo-microscopy. Electron cryo-tomography has provided new insights into the supra-molecular arrangement of eukaryotic ATP synthases within mitochondria and mass-spectrometry has started to identify specifically bound lipids presumed to be essential for function. Taken together these molecular snapshots show that nano-scale rotary engines have much in common with basic design principles of man made machines from the function of individual "machine elements" to the requirement of the right "fuel" and "oil" for different types of motors.

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
自引率
0.00%
发文量
0
×
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:481959085
Book学术官方微信