The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.

ABSTRACT: Clostridium difficile is a burden to healthcare systems around the world, causing tens of thousands of deaths annually. The S-layer of the bacterium, a layer of protein found of the surface of cells, has received a significant amount of attention over the past two decades as a potential target to combat the growing threat presented by C. difficile infections. The S-layer contains a wide range of proteins, each of which possesses three cell wall-binding domains, while many also possess a "functional" region. Here, we present the high resolution structure of the functional region of one such protein, Cwp19 along with preliminary functional characterisation of the predicted glycoside hydrolase. Cwp19 has a TIM barrel fold and appears to possess a high degree of substrate selectivity. The prot

SUBMITTER: Bradshaw WJ 

PROVIDER: S-EPMC5765458 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature