Conformation of the myosin motor during force generation in skeletal muscle

M Irving; G Piazzesi; L Lucii; Y B Sun; J J Harford; I M Dobbie; M A Ferenczi; M Reconditi; V Lombardi

doi:10.1038/75890

Conformation of the myosin motor during force generation in skeletal muscle

M Irving, G Piazzesi, L Lucii, Y B Sun, J J Harford, I M Dobbie, M A Ferenczi, M Reconditi, V Lombardi

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Abstract

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.

Original language	English
Pages (from-to)	482 - 485
Number of pages	4
Journal	Nature Structural Biology
Volume	7
Issue number	6
DOIs	https://doi.org/10.1038/75890
Publication status	Published - Jun 2000

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abstract = "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.",

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AU - Irving, M

AU - Piazzesi, G

AU - Lucii, L

AU - Sun, Y B

AU - Harford, J J

AU - Dobbie, I M

AU - Ferenczi, M A

AU - Reconditi, M

AU - Lombardi, V

PY - 2000/6

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AB - 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.

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Conformation of the myosin motor during force generation in skeletal muscle

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