Switch movements and the myosin crossbridge stroke

Switch movements and the myosin crossbridge stroke
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开关运动和肌球蛋白横桥行程

DOI:
10.1007/s10974-005-9004-y
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发表时间:
2005
影响因子:
2.7
通讯作者:
Clive R. Bagshaw
Clive R. Bagshaw
中科院分区:
生物学3区
文献类型:
--
作者:
A. Málnási;Jane L. Dickens;W. Zeng;Clive R. Bagshaw

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来自盘基网柄藻的肌球蛋白II马达已经被工程化以在策略位置含有单个色氨酸残基以探测开关1和开关2的运动。W501处的色氨酸残基探测中继螺旋的运动,并间接报告开关2的运动。该探针表明,当γ-磷酸位置被占据时,开关2的打开状态和关闭状态之间存在平衡。肌动蛋白似乎并没有直接对这种平衡产生很大影响,但通过开关1产生间接影响。后一区域已通过在位置239和242处引入色氨酸残基来探测。肌动球蛋白ATP酶在溶液中的动力学进行了讨论,最近的crossbridge模型的基础上高分辨率的晶体结构。
The myosin II motor from Dictyostelium discoideum has been engineered to contain single tryptophan residues at strategic locations to probe movements of switch 1 and switch 2. The tryptophan residue at W501 probes movement of the relay helix and indirectly reports on switch 2 movement. This probe suggests that there is an equilibrium between the switch 2 open- and closed-states when the γ-phosphate position is occupied. Actin does not appear to greatly affect this equilibrium directly, but has indirect influence via switch 1. The latter region has been probed by introducing tryptophan residues at positions 239 and 242. The kinetics of the actomyosin ATPase in solution is discussed with respect to recent crossbridge models based on high-resolution crystal structures.
含有单个色氨酸的平滑肌肌球蛋白突变体揭示了肌动蛋白结合界面上的分子相互作用。
DOI: 10.1073/pnas.95.22.12944
发表时间: 1998
影响因子: 11.1
作者:
Yengo,CM;Fagnant,PM;Chrin,L;Rovner,AS;Berger,CL
通讯作者: Berger,CL
DOI: --
发表时间: 1995-04
影响因子: 3.4
作者:
R. Yount;D. Lawson;I. Rayment
通讯作者: R. Yount;D. Lawson;I. Rayment