Conformation of the myosin motor during force generation in skeletal muscle

被引:80
作者
Irving, M
Piazzesi, G
Lucii, L
Sun, YB
Harford, JJ
Dobbie, IM
Ferenczi, MA
Reconditi, M
Lombardi, V
机构
[1] Kings Coll London, Sch Biomed Sci, London SE1 1UL, England
[2] Univ Florence, Dipartimento Sci Fisiol, I-50134 Florence, Italy
[3] Natl Inst Med Res, London NW7 1AA, England
来源
NATURE STRUCTURAL BIOLOGY | 2000年 / 7卷 / 06期
基金
英国医学研究理事会;
关键词
D O I
10.1038/75890
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
Myosin motors drive muscle contraction, cytokinesis and cell locomotion, and members of the myosin superfamily have been implicated in an increasingly diverse range of cell functions. Myosin can displace a bound actin filament several nanometers in a single interaction. Crystallographic studies suggest that this 'working stroke' involves bending of the myosin head between its light chain and catalytic domains. Here we used X-ray fiber diffraction to test the crystallographic model and measure the interdomain bending during force generation in an intact single muscle fiber. The observed bending has two components: an elastic distortion and an active rotation that generates force. The average bend of the force-generating myosin heads in a muscle fiber is intermediate between those in crystal structures with different bound nucleotides, and the C-terminus of the head is displaced by 7 nm along the actin filament axis compared with the in vitro conformation seen in the absence of nucleotide.
引用
收藏
页码:482 / 485
页数:4
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