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  • 标题:Structure of the mitochondrial F1 ATPase at 9-A resolution
  • 本地全文:下载
  • 作者:L M Amzel ; M McKinney ; P Narayanan
  • 期刊名称:Proceedings of the National Academy of Sciences
  • 印刷版ISSN:0027-8424
  • 电子版ISSN:1091-6490
  • 出版年度:1982
  • 卷号:79
  • 期号:19
  • 页码:5852-5856
  • DOI:10.1073/pnas.79.19.5852
  • 语种:English
  • 出版社:The National Academy of Sciences of the United States of America
  • 摘要:The soluble portion (F1 ATPase) of the mitochondrial ATP-synthesizing system is a multisubunit enzyme of molecular weight 380,000. It is composed of five different subunits, alpha, beta, gamma, and epsilon. The subunit stoichiometry is not known but there are strong suggestions that it is alpha 3 beta 3 gamma delta epsilon. We have determined the three-dimensional structure of the F1 ATPase of rat liver mitochondria to 9-A resolution by using x-ray diffraction techniques. The molecule appears to be formed by two equivalent halves, each formed by three regions of approximately equal size. These regions form a distorted hexagonal or octahedral arrangement. None of the regions form closed symmetrical trimers in the complex. It is proposed that, if the subunit stoichiometry is alpha 3 beta 3 gamma delta epsilon, the major subunits exist in at least two different environments in the complex. In this arrangement, the different copies of the major subunits are functionally not equivalent. This observation appears to offer a natural explanation of the complicated binding and labeling data of F1 ATPases.
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