Abstract
Troponin, a Ca2+-sensitive complex, regulates the motions of tropomyosin on the thin filaments in many muscles. It has three subunits, each with a different architecture and function: TnC binds Ca2+; Tnl binds to actin and inhibits contraction; and TnT binds one complex to each tropomyosin molecule1,2. The troponin complex has an elongated shape with TnC and Tnl forming a globular 'head' region and TnT a long (-160 Å) 'tail'3. TnT binds to two widely separated regions of tropomyosin: the head region of the complex is near Cys 190 of tropomyosin and the tail region is near the overlapping joint that links the tropomyosin molecules into filaments4. Here we report the X-ray structure determination at 17 Å resolution of glutaraldehyde-treated tropomyosin crystals in which native troponin complex or fragments of TnT have been bound. Our results show that the amino-terminal tail end of TnT spans the head-to-tail joint of the tropomyosin filaments, and that the 'head' region of the whole troponin complex binds -200 A away near residues 150–180 of the tropomyosin molecule.
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White, S., Cohen, C. & Phillips Jr, G. Structure of co-crystals of tropomyosin and troponin. Nature 325, 826–828 (1987). https://doi.org/10.1038/325826a0
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DOI: https://doi.org/10.1038/325826a0
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