期刊
FEBS JOURNAL
卷 284, 期 24, 页码 4343-4357出版社
WILEY
DOI: 10.1111/febs.14310
关键词
bacterial adhesion; cell wall; Clostridium difficile; colitis; crystal structure
资金
- Public Health England (PHE, Porton Down, England)
- University of Bath
- Medical Research Council (UK) [MR/K027123/1]
- MRC [MR/K027123/1] Funding Source: UKRI
- Medical Research Council [MR/K027123/1] Funding Source: researchfish
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. DatabaseStructural data are available in the PDB under the accession numbers and .
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