STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA

被引：2731

作者：

ABRAHAMS, JP ^{[1
]}

LESLIE, AGW ^{[1
]}

LUTTER, R ^{[1
]}

WALKER, JE ^{[1
]}

机构：

[1] MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND

来源：

NATURE | 1994年 / 370卷 / 6491期

关键词：

D O I：

10.1038/370621a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

In the crystal structure of bovine mitochondrial F-1-ATPase determined at 2.8 Angstrom resolution, the three catalytic beta-subunits differ in conformation and in the bound nucleotide. The structure supports a catalytic mechanism in intact ATP synthase in which the three catalytic subunits are in different states of the catalytic cycle at any instant. Interconversion of the states may be achieved by rotation of the alpha(3) beta(3) subassembly relative to an alpha-helical domain of the gamma-subunit.

引用

页码：621 / 628

页数：8

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