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.
Original language | English |
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Pages (from-to) | 4343-4357 |
Number of pages | 15 |
Journal | FEBS Journal |
Volume | 284 |
Issue number | 24 |
Early online date | 17 Nov 2017 |
DOIs | |
Publication status | Published - 18 Dec 2017 |
Keywords
- Bacterial Proteins
- Catalytic Domain
- Clostridium difficile
- Crystallography, X-Ray
- Glycoside Hydrolases
- Hydrolysis
- Membrane Glycoproteins
- Models, Molecular
- Peptidoglycan
- Protein Conformation
- Protein Domains
- Journal Article
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