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To gain insight into the relationship between protein structure and mechanical stability, single molecule force spectroscopy experiments on proteins with diverse structure and topology are needed. Here, we measured the mechanical stability of extender domains of two bacterial adhesins  Mp AFP and  Mh Lap, in an atomic force microscope. We find that both proteins are remarkably stable to pulling forces between their N- and C- terminal ends. At a pulling speed of 1 μm/s, the  Mp AFP extender domain fails at an unfolding force  F  u  = 348 ± 37 pN and  Mh Lap at  F  u  = 306 ± 51 pN in buffer with 10 mM Ca 2+ . These forces place both extender domains well above the mechanical stability of many other β-sandwich domains in mechanostable proteins. We propose that the increased stability of  Mp AFP and  Mh Lap is due to a combination of both hydrogen bonding between parallel terminal strands and intra-molecular coordination of calcium ions.

Unusually high mechanical stability of bacterial adhesin extender domains having calcium clamps