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C2 domain conformational changes in phospholipase C-δ1

Nature Structural Biology volume 3, pages 788–795 (1996)Cite this article

Abstract

The structure of the PH-domain truncated core of rat phosphoinositide-specific phospholipase C-δ1 has been determined at 2.4 Å resolution and compared to the structure previously determined in a different crystal form. The stereochemical relationship between the EF, catalytic, and C2 domains is essentially identical. The Ca2+ analogue Sm3+ binds at two sites between the jaws of the C2 domain. Sm3+ binding ejects three lysine residues which bridge the gap between the jaws and occupy the Ca2+ site in the apoenzyme, triggering a conformational change in the jaws. The distal sections of the C2 jaws move apart, opening the mouth by 9 Å and creating a gap large enough to bind a phospholipid headgroup.

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Authors and Affiliations

  1. Laboratory of Molecular Biology, National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Building 5, Rm 435, Bethesda, Maryland, 20892-0580, USA

    Jay A. Grobler & James H. Hurley

  2. Centre for Protein Engineering, MRC Centre, Hills Rd., Cambridge, CB2 2QH, UK

    Lars-Oliver Essen & Roger L. Williams

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  2. Lars-Oliver Essen
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  3. Roger L. Williams
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  4. James H. Hurley
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Grobler, J., Essen, LO., Williams, R. et al. C2 domain conformational changes in phospholipase C-δ1. Nat Struct Mol Biol 3, 788–795 (1996). https://doi.org/10.1038/nsb0996-788

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