NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles

被引:40
作者
Matthey, U
Kaim, G
Braun, D
Wüthrich, K
Dimroth, P [1 ]
机构
[1] ETH Zentrum, Inst Mikrobiol, CH-8092 Zurich, Switzerland
[2] ETH Zurich, Inst Mol Biol & Biophys, CH-8093 Zurich, Switzerland
来源
EUROPEAN JOURNAL OF BIOCHEMISTRY | 1999年 / 261卷 / 02期
关键词
ATP synthase; NMR structure; Propionigenium modestum; subunit c;
D O I
10.1046/j.1432-1327.1999.00288.x
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 structure of the Na+, Li+ or H+-binding c subunit of the ATP synthase from Propionigenium modestum was studied by NMR. Subunit c in dodecylsulphate micelles consists of four alpha-helical segments, I-IV, that are connected by short linker peptides with non-regular secondary structures. We propose that helices I (V4-I26) and IV (I69-V85) are membrane-spanning structures, and that helices II and III and the intervening hydrophilic loop are located in the cytoplasm. The Na+-binding residues Q32, E65 and S66 are located in the I-->II and III-->IV helix connections, probably near the membrane surface on the cytoplasmic side.
引用
收藏
页码:459 / 467
页数:9
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