ATP synthase's second stalk comes into focus

被引:126
作者
Wilkens, S [1 ]
Capaldi, RA [1 ]
机构
[1] Univ Oregon, Inst Mol Biol, Eugene, OR 97403 USA
关键词
D O I
10.1038/29908
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
Almost all the adenosine triphosphate (ATP, the predominant energy-transfer mediator in living organisms) used by cells is made by ATP synthases, which have two parts known as F1 and FO. These enzymes are found in bacterial plasma membranes, chloroplast thylakoid membranes and mitochondrial inner membranes; they function as rotary motors, coupling nucleotide binding in the F1 part to proton translocation by the transmembrane FO part1,2. Here we present cryoelectron microscopy images showing details of the connection between the F1 and FO parts of the enzyme.
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页码:29 / 29
页数:1
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