ArticlePloS one2017
Unusually high mechanical stability of bacterial adhesin extender domains having calcium clamps.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Calpain small subunit homodimerization is robust and calcium-independent.FEBS letters · 2026Article
- Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.Nature communications · 2025Article
- Mechanical forces and ligand binding modulateLife science alliance · 2025Article
- Essential role of calcium in extending RTX adhesins to their target.Journal of structural biology: X · 2020Article
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5 authors.
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Abstract
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 MpAFP and MhLap, 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 MpAFP extender domain fails at an unfolding force Fu = 348 ± 37 pN and MhLap at Fu = 306 ± 51 pN in buffer with 10 mM Ca2+. 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 MpAFP and MhLap is due to a combination of both hydrogen bonding between parallel terminal strands and intra-molecular coordination of calcium ions.
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