5oq2

Publication Abstract from PubMed

Clostridium difficile is a burden to health care 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 possess 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. This article is protected by copyright. All rights reserved.

The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.,Bradshaw WJ, Kirby JM, Roberts AK, Shone CC, Acharya KR FEBS J. 2017 Oct 30. doi: 10.1111/febs.14310. PMID:29083543^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.