Abstract
We have previously proposed that allosteric regulation causes some receptors to form catch bonds, which are strengthened rather than weakened by mechanical force. Here we describe a crystal structure of the catch-bond forming bacterial adhesive protein FimH in native fimbrial tips that is dramatically different that previous structures of FimH. The new structure shows how a neighboring domain allosterically inhibits the adhesive domain. In previous crystal structures, the adhesive domain was pre-activated by prevention of these native inter-domain contacts.
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