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Calcium stabilizes the strongest protein fold

Author

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  • Lukas F. Milles

    (Ludwig-Maximilians-University)

  • Eduard M. Unterauer

    (Ludwig-Maximilians-University)

  • Thomas Nicolaus

    (Ludwig-Maximilians-University)

  • Hermann E. Gaub

    (Ludwig-Maximilians-University)

Abstract

Staphylococcal pathogens adhere to their human targets with exceptional resilience to mechanical stress, some propagating force to the bacterium via small, Ig-like folds called B domains. We examine the mechanical stability of these folds using atomic force microscopy-based single-molecule force spectroscopy. The force required to unfold a single B domain is larger than 2 nN – the highest mechanostability of a protein to date by a large margin. B domains coordinate three calcium ions, which we identify as crucial for their extreme mechanical strength. When calcium is removed through chelation, unfolding forces drop by a factor of four. Through systematic mutations in the calcium coordination sites we can tune the unfolding forces from over 2 nN to 0.15 nN, and dissect the contribution of each ion to B domain mechanostability. Their extraordinary strength, rapid refolding and calcium-tunable force response make B domains interesting protein design targets.

Suggested Citation

  • Lukas F. Milles & Eduard M. Unterauer & Thomas Nicolaus & Hermann E. Gaub, 2018. "Calcium stabilizes the strongest protein fold," Nature Communications, Nature, vol. 9(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07145-6
    DOI: 10.1038/s41467-018-07145-6
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