Myosin Motor Domain Lever Arm Rotation Is Coupled to ATP Hydrolysis†

Biochemistry ◽  
2000 ◽  
Vol 39 (40) ◽  
pp. 12330-12335 ◽  
Author(s):  
Stefan Highsmith ◽  
Katherine Polosukhina ◽  
Don Eden
Keyword(s):  
Atp Hydrolysis ◽  
Motor Domain ◽  
Myosin Motor ◽  
Lever Arm ◽  
Myosin Motor Domain

scholarly journals Dynamics of actomyosin interactions in relation to the cross-bridge cycle

2004 ◽  
Vol 359 (1452) ◽  
pp. 1843-1855 ◽  
Author(s):  
K. C. Holmes ◽  
D. R. Trentham ◽  
R. Simmons ◽  
Wei Zeng ◽  
Paul B. Conibear ◽  
...  
Keyword(s):  
Motor Domain ◽  
Actin Binding ◽  
Kinetic Measurements ◽  
Product Release ◽  
Myosin Motor ◽  
Cross Bridge ◽  
Lever Arm ◽  
Arm Position ◽  
Myosin Motor Domain ◽  
The Cross

Transient kinetic measurements of the actomyosin ATPase provided the basis of the Lymn–Taylor model for the cross–bridge cycle, which underpins current models of contraction. Following the determination of the structure of the myosin motor domain, it has been possible to introduce probes at defined sites and resolve the steps in more detail. Probes have been introduced in the Dicytostelium myosin II motor domain via three routes: (i) single tryptophan residues at strategic locations throughout the motor domain; (ii) green fluorescent protein fusions at the N and C termini; and (iii) labelled cysteine residues engineered across the actin–binding cleft. These studies are interpreted with reference to motor domain crystal structures and suggest that the tryptophan (W501) in the relay loop senses the lever arm position, which is controlled by the switch 2 open–to–closed transition at the active site. Actin has little effect on this process per se . A mechanism of product release is proposed in which actin has an indirect effect on the switch 2 and lever arm position to achieve mechanochemical coupling. Switch 1 closing appears to be a key step in the nucleotide–induced actin dissociation, while its opening is required for the subsequent activation of product release. This process has been probed with F239W and F242W substitutions in the switch 1 loop. The E706K mutation in skeletal myosin IIa is associated with a human myopathy. To simulate this disease we investigated the homologous mutation, E683K, in the Dictyostelium myosin motor domain.

scholarly journals Coupling of protein surface hydrophobicity change to ATP hydrolysis by myosin motor domain

1997 ◽  
Vol 72 (1) ◽  
pp. 18-23 ◽  
Author(s):  
M. Suzuki ◽  
J. Shigematsu ◽  
Y. Fukunishi ◽  
Y. Harada ◽  
T. Yanagida ◽  
...  
Keyword(s):  
Atp Hydrolysis ◽  
Surface Hydrophobicity ◽  
Motor Domain ◽  
Protein Surface ◽  
Myosin Motor ◽  
Myosin Motor Domain ◽  
Protein Surface Hydrophobicity

scholarly journals The structure of the actin-smooth muscle myosin motor domain complex in the rigor state

2017 ◽  
Vol 200 (3) ◽  
pp. 325-333 ◽  
Author(s):  
Chaity Banerjee ◽  
Zhongjun Hu ◽  
Zhong Huang ◽  
J. Anthony Warrington ◽  
Dianne W. Taylor ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Smooth Muscle Myosin ◽  
Motor Domain ◽  
Myosin Motor ◽  
Rigor State ◽  
Myosin Motor Domain ◽  
Muscle Myosin
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