Key result
The essential light chain of myosin stabilizes the arm, and its conformational flexibility is involved in coupling ATP hydrolysis and rotation of the arm.
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Design
Review
This review summarizes the structural and functional roles of the essential light chain of myosin, emphasizing its conformational flexibility and interactions with actin.
The review summarizes recent data on the structure and functions of the essential light chain of myosin. The essential light chain of myosin is known to stabilize the arm. Consistent with the model of the shift of the dynamic population of conformations, the conformational flexibility of the essential light chain of myosin is emphasized, which opens the way to the determination of its novel functions. The assumption is substantiated that the interaction between the C-terminal domain of the essential light chain and the N-terminal subdomain of the heavy chain of myosin is involved in the coupling of ATP hydrolysis and rotation of the arm. The recent data indicate that the isoforms of the essential light chain with the additional N-terminal peptide are capable of interacting with actin and the src-homologous domain 3 of myosin. The structural aspects of these interactions and the modulatory role of the isoforms of the essential light chain of myosin are discussed.
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Dmitry S. Ushakov (2008) reported a review. The essential light chain of myosin stabilizes the arm, and its conformational flexibility is involved in coupling ATP hydrolysis and rotation of the arm.
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