RMSD analysis of structures of the bacterial protein FimH identifies five conformations of its lectin domain.

ABSTRACT: FimH is a bacterial adhesin protein located at the tip of Escherichia coli fimbria that functions to adhere bacteria to host cells. Thus, FimH is a critical factor in bacterial infections such as urinary tract infections and is of interest in drug development. It is also involved in vaccine development and as a model for understanding shear-enhanced catch bond cell adhesion. To date, over 60 structures have been deposited in the Protein Data Bank showing interactions between FimH and mannose ligands, potential inhibitors, and other fimbrial proteins. In addition to providing insights about ligand recognition and fimbrial assembly, these structures provide insights into conformational changes in the two domains of FimH that are critical for its function. To gain further insights into these

SUBMITTER: Magala P 

PROVIDER: S-EPMC7058522 | biostudies-literature | 2020 Apr

REPOSITORIES: biostudies-literature