1. The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
- Author
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Bradshaw, William J., Kirby, Jonathan M., Roberts, April K., Shone, Clifford C., and Acharya, K. Ravi
- Subjects
GLYCOSIDASES ,CLOSTRIDIOIDES difficile ,MOLECULAR structure ,BACTERIAL proteins ,BACTERIAL adhesion ,BACTERIAL cell walls - 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 protein also exhibits peptidoglycan hydrolase activity, an order of magnitude slower than that of lysozyme and is the first member of glycoside hydrolase-like family 10 to be characterised. This research goes some way to understanding the role of Cwp19 in the S-layer of C. difficile. Database Structural data are available in the PDB under the accession numbers and . [ABSTRACT FROM AUTHOR]
- Published
- 2017
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