Requirement of Domain-Domain Interaction for Conformational Change and Functional ATP Hydrolysis in Myosin

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Structured PICO

Population

Myosin molecules (in vivo and in vitro models)

Intervention

F482A mutation and F482A/G680F double mutation in myosin

Comparator

Wild-type myosin (implied)

Outcome

Motor activities, ATP hydrolysis, and conformational changes (transition from open to closed state)surrogate

Contact between side chains of Phe-482 and Gly-680 in myosin is essential for coordinated conformational changes and subsequent ATP hydrolysis.

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Pinpoints essential myosin side-chain interactions for ATP hydrolysis; leaves open relevance to human cardiomyopathies without further validation.

Ito et al. (2003) studied this question.

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Pinpoints essential myosin side-chain interactions for ATP hydrolysis; leaves open relevance to human cardiomyopathies without further validation.