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

页码：459 / 467

页数：9