Kinesin and Myosin ATPases: Variations on a Theme [and Discussion]

The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less is known about kinesin, but many of its major prop...

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Bibliographic Details
Published in:Philosophical transactions of the Royal Society of London. Series B. Biological sciences 1992-04, Vol.336 (1276), p.13-18
Main Authors: Hackney, David D., Johnson, K. A., Hackney, D. D., Holmes, K. C., M.-F. Carlier, Elliott, G. F., Burton, K., Trentham, D. R., Cremo, C.
Format: Article
Language:English
Subjects:
Actins
Active sites
Adenosine triphosphatases
Adenosine Triphosphate - metabolism
Dimers
Enzymes
Hydrolysis
Kinesin - chemistry
Kinesin - metabolism
Microtubules
Microtubules - metabolism
Molecular Structure
Molecules
Motors
Myosins - chemistry
Myosins - metabolism
Oxygen
Protein Conformation
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Summary:The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less is known about kinesin, but many of its major properties are similar to those of myosin. Both enzymes have two catalytic head groups at the end of a long $\alpha $-helical rod. The head groups contain the sites for ATP hydrolysis and interaction with their respective partners for movement (microtubules or F-actin). In each case the binding and hydrolysis of ATP is rapid and the steady state ATPase rate is limited by a slow step in the region of product release. This slow release of product is accelerated by interaction with actin or microtubules coupled to changes in binding affinity. As there is no evidence for a close evolutionary link between kinesin and myosin, these and other similarities may represent convergence to set of common functional properties which are constrained by the requirements of protein structure and the use of ATP hydrolysis as a source of energy. It will be of particular interest to determine if these common properties are also shared by the large number of divergent proteins which have recently been discovered to possess a domain which is homologous to the head group of kinesin.
ISSN:0962-8436
1471-2970
DOI:10.1098/rstb.1992.0038