Mechanism of allosteric propagation across a β-sheet structure investigated by molecular dynamics simulations.

ABSTRACT: The bacterial adhesin FimH consists of an allosterically regulated mannose-binding lectin domain and a covalently linked inhibitory pilin domain. Under normal conditions, the two domains are bound to each other, and FimH interacts weakly with mannose. However, under tensile force, the domains separate and the lectin domain undergoes conformational changes that strengthen its bond with mannose. Comparison of the crystallographic structures of the low and the high affinity state of the lectin domain reveals conformational changes mainly in the regulatory inter-domain region, the mannose binding site and a large β sheet that connects the two distally located regions. Here, molecular dynamics simulations investigated how conformational changes are propagated within and between different region

SUBMITTER: Interlandi G 

PROVIDER: S-EPMC5084802 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature