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Solution structure of calcium-free calmodulin

Nature Structural Biology volume 2, pages 768–776 (1995)Cite this article

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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Authors and Affiliations

  1. Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, 20892-0520, USA

    Hitoshi Kuboniwa, Nico Tjandra, Stephan Grzesiek & Ad Bax

  2. Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, Maryland, 20892-0520, USA

    Hao Ren & Claude B. Klee

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  1. Hitoshi Kuboniwa
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  2. Nico Tjandra
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  4. Hao Ren
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  5. Claude B. Klee
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  6. Ad Bax
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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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