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

William J Bradshaw, Jonathan M Kirby, April K. Roberts, Clifford C. Shone, K Ravi Acharya

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

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 languageEnglish
Pages (from-to)4343-4357
Number of pages15
JournalFEBS Journal
Volume284
Issue number24
Early online date17 Nov 2017
DOIs
Publication statusPublished - 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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