Calcium stabilizes the strongest protein fold

Lukas F. Milles (), Eduard M. Unterauer, Thomas Nicolaus and Hermann E. Gaub ()
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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

Nature Communications, 2018, vol. 9, issue 1, 1-10

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-07145-6

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