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

DOI: 10.1111/febs.14310 DOI Help

Authors: William J. Bradshaw (University of Bath) , Jonathan M. Kirby (Public Health England) , April K. Roberts (Public Health England) , Clifford C. Shone (Public Health England) , K. Ravi Acharya (University of Bath)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: The Febs Journal , VOL 37

State: Published (Approved)
Published: November 2017
Diamond Proposal Number(s): 7131 , 8922

Open Access Open Access

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.

Journal Keywords: bacterial adhesion; cell wall; Clostridium difficile; colitis; crystal structure

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Documents:
Bradshaw_et_al-2017-The_FEBS_Journal.pdf

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