Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1

被引:101
|
作者
Yagi, Hiromasa
Kajiwara, Nobumoto
Tanaka, Hideaki
Tsukihara, Tornitake
Kato-Yamada, Yasuyuki
Yoshida, Masasuke
Akutsu, Hideo
机构
[1] Osaka Univ, Inst Prot Res, Suita, Osaka 5650871, Japan
[2] Rikkyo St Paul Univ, Coll Sci, Tokyo 1718501, Japan
[3] Tokyo Inst Technol, Chem Resources Lab, Yokohama, Kanagawa 2268503, Japan
关键词
ATP hydrolysis; ATP-binding motif; ATPase regulation; ATP synthase; F-1; rotation;
D O I
10.1073/pnas.0701045104
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
The epsilon subunit of bacterial and chloroplast FoF1-ATP synthases modulates their ATP hydrolysis activity. Here, we report the crystal structure of the ATP-bound E subunit from a thermophilic Bacillus PS3 at 1.9-angstrom resolution. The C-terminal two a-helices were folded into a hairpin, sitting on the 13 sandwich structure, as reported for Escherichia coli. A previously undescribed ATP binding motif, l(L)DXXRA, recognizes ATP together with three arginine and one glutamate residues. The E. coli e subunit binds ATP in a similar manner, as judged on NMR. We also determined solution structures of the C-terminal domain of the PS3 E subunit and relaxation parameters of the whole molecule by NMR. The two helices fold into a hairpin in the presence of ATIP but extend in the absence of ATP. The latter structure has more helical regions and is much more flexible than the former. These results suggest that the e C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of FoF1-ATP synthase.
引用
收藏
页码:11233 / 11238
页数:6
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