Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution

Xie, X.; Harrison, D. H.; Schlichting, Ilme; Sweet, Robert M.; Kalabokis, V. N.; Szent−Gyorgyi, A. G.; Cohen, C.

doi:10.1038/368306a0

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Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution

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Schlichting, Ilme
Photoreceptors, Max Planck Institute for Medical Research, Max Planck Society;
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

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https://www.nature.com/nature/journal/v368/n6469/pdf/368306a0.pdf
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Citation

Xie, X., Harrison, D. H., Schlichting, I., Sweet, R. M., Kalabokis, V. N., Szent−Gyorgyi, A. G., et al. (1994). Structure of the regulatory domain of scallop myosin at 2.8 Ä resolution. Nature, 368(6469), 306-312. doi:10.1038/368306a0.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0019-A930-5

Abstract

The regulatory domain of scallop myosin is a three-chain protein complex that switches on this motor in response to Ca2+ binding. This domain has been crystallized and the structure solved to 2.8 Å resolution. Side-chain interactions link the two light chains in tandem to adjacent segments of the heavy chain bearing the IQ-sequence motif. The Ca2+-binding site is a novel EF-hand motif on the essential light chain and is stabilized by linkages involving the heavy chain and both light chains, accounting for the requirement of all three chains for Ca2+ binding and regulation in the intact myosin molecule.