A BARREL IN THE STALK

被引:9
作者
DUNN, SD
机构
[1] Department of Biochemistry, University of Western Ontario, London, ON
来源
NATURE STRUCTURAL BIOLOGY | 1995年 / 2卷 / 11期
关键词
D O I
10.1038/nsb1195-915
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
The first sighting of the ATP synthase epsilon subunit structure-a vital component of the stalk involved in energy transmission between membrane-bound and cytoplasmic portions of the synthase-provides intriguing hints about its possible mode of action.
引用
收藏
页码:915 / 918
页数:4
相关论文
共 17 条
[1]   STRUCTURE AT 2.8-ANGSTROM RESOLUTION OF F1-ATPASE FROM BOVINE HEART-MITOCHONDRIA [J].
ABRAHAMS, JP ;
LESLIE, AGW ;
LUTTER, R ;
WALKER, JE .
NATURE, 1994, 370 (6491) :621-628
[2]  
DALLMANN HG, 1992, J BIOL CHEM, V267, P18953
[3]  
DUNCAN TM, 1995, IN PRESS P NATN ACAD
[4]  
DUNN SD, 1982, J BIOL CHEM, V257, P7354
[5]  
DUNN SD, 1992, J BIOL CHEM, V267, P7630
[6]  
GIRVIN ME, 1995, BIOCHEMISTRY-US, V33, P665
[7]  
GRESSER MJ, 1982, J BIOL CHEM, V257, P2030
[8]   THE MITOCHONDRIAL ATP SYNTHASE INHIBITOR PROTEIN BINDS NEAR THE C-TERMINUS OF THE F1 BETA-SUBUNIT [J].
JACKSON, PJ ;
HARRIS, DA .
FEBS LETTERS, 1988, 229 (01) :224-228
[9]  
KUKI M, 1988, J BIOL CHEM, V263, P17437
[10]   NUCLEOTIDE-DEPENDENT AND DICYCLOHEXYLCARBODIIMIDE-SENSITIVE CONFORMATIONAL-CHANGES IN THE EPSILON-SUBUNIT OF ESCHERICHIA-COLI ATP SYNTHASE [J].
MENDELHARTVIG, J ;
CAPALDI, RA .
BIOCHEMISTRY, 1991, 30 (45) :10987-10991