A CRYOELECTRON MICROSCOPY STUDY OF THE INTERACTION OF THE ESCHERICHIA-COLI F1-ATPASE WITH SUBUNIT-B DIMER

被引:25
作者
WILKENS, S
DUNN, SD
CAPALDI, RA
机构
[1] UNIV OREGON,INST MOLEC BIOL,EUGENE,OR 97403
[2] UNIV WESTERN ONTARIO,DEPT BIOCHEM,LONDON N6A 5C1,ON,CANADA
关键词
CRYOELECTRON MICROSCOPY; F1-ATPASE; ATP SYNTHASE; B SUBUNIT;
D O I
10.1016/0014-5793(94)01059-5
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A complex between the Escherichia coli F-1-ATPase and a truncated form of the ECF(0)-b subunit was formed and examined by cryoelectron microscopy in amorphous ice. Image analysis of single particles in the hexagonal projection revealed that the polar domain of the b subunit interacts with a beta subunit different from the one which interacts with the epsilon subunit. The cavity in the enzyme, visible in the hexagonal projection, is not filled by the b polypeptide, therefore leaving enough room for extensive conformational changes of the gamma and epsilon subunits within the native F1F0 complex.
引用
收藏
页码:37 / 40
页数:4
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