F1-ATPase Changes Its Conformations upon Phosphate Release*
F1-ATPase Changes Its Conformations upon Phosphate Release*
复制标题
F1-ATP 酶在磷酸盐释放时改变其构象*
DOI:
10.1074/jbc.m110297200
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发表时间:
2002
期刊:
影响因子:
--
通讯作者:
Masasuke Yoshida
中科院分区:
文献类型:
--
作者:
T. Masaike;E. Muneyuki;H. Noji;K. Kinosita;Masasuke Yoshida
Motor proteins, myosin, and kinesin have γ-phosphate sensors in the switch II loop that play key roles in conformational changes that support motility. Here we report that a rotary motor, F1-ATPase, also changes its conformations upon phosphate release. The tryptophan mutation was introduced into Arg-333 in the β subunit of F1-ATPase from thermophilic Bacillus PS3 as a probe of conformational changes. This residue interacts with the switch II loop (residues 308–315) of the β subunit in a nucleotide-bound conformation. The addition of ATP to the mutant F1subcomplex α3β(R333W)3γ caused transient increase and subsequent decay of the Trp fluorescence. The increase was caused by conformational changes on ATP binding. The rate of decay agreed well with that of phosphate release monitored by phosphate-binding protein assays. This is the first evidence that the β subunit changes its conformation upon phosphate release, which may share a common mechanism of exerting motility with other motor proteins.
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DOI:
10.1042/bj3301037
发表时间:
1998
期刊:
The Biochemical journal
影响因子:
--
作者:
Milgrom,YM;Murataliev,MB;Boyer,PD
通讯作者:
Boyer,PD
DOI:
10.1016/s0021-9258(20)80703-0
发表时间:
1993-09
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
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通讯作者:
J. Weber;S. Wilke-Mounts;Rita S. F. Lee;E. Grell;A. E. Senior
DOI:
10.1021/bi981089c
发表时间:
1998
期刊:
Biochemistry.
影响因子:
--
作者:
Weber,J;Wilke-Mounts,S;Hammond,ST;Senior,AE
通讯作者:
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DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Grubmeyer,C;Cross,RL;Penefsky,HS
通讯作者:
Penefsky,HS
DOI:
10.1073/pnas.92.24.10964
发表时间:
1995-11-21
影响因子:
11.1
作者:
DUNCAN, TM;BULYGIN, VV;CROSS, RL
通讯作者:
CROSS, RL