Abstract
The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca2+-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel β-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca2+-free N-terminal domain of troponin C.
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Kuboniwa, H., Tjandra, N., Grzesiek, S. et al. Solution structure of calcium-free calmodulin. Nat Struct Mol Biol 2, 768–776 (1995). https://doi.org/10.1038/nsb0995-768
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DOI: https://doi.org/10.1038/nsb0995-768
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