Cargando…

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

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 co...

Descripción completa

Detalles Bibliográficos
Autores principales: Bradshaw, William J., Kirby, Jonathan M., Roberts, April K., Shone, Clifford C., Acharya, K. Ravi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5765458/
https://www.ncbi.nlm.nih.gov/pubmed/29083543
http://dx.doi.org/10.1111/febs.14310
_version_ 1783292235354210304
author Bradshaw, William J.
Kirby, Jonathan M.
Roberts, April K.
Shone, Clifford C.
Acharya, K. Ravi
author_facet Bradshaw, William J.
Kirby, Jonathan M.
Roberts, April K.
Shone, Clifford C.
Acharya, K. Ravi
author_sort Bradshaw, William J.
collection PubMed
description 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. DATABASE: Structural data are available in the PDB under the accession numbers 5OQ2 and 5OQ3.
format Online
Article
Text
id pubmed-5765458
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher John Wiley and Sons Inc.
record_format MEDLINE/PubMed
spelling pubmed-57654582018-02-01 The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile Bradshaw, William J. Kirby, Jonathan M. Roberts, April K. Shone, Clifford C. Acharya, K. Ravi FEBS J Original Articles 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. DATABASE: Structural data are available in the PDB under the accession numbers 5OQ2 and 5OQ3. John Wiley and Sons Inc. 2017-11-17 2017-12 /pmc/articles/PMC5765458/ /pubmed/29083543 http://dx.doi.org/10.1111/febs.14310 Text en © 2017 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. This is an open access article under the terms of the Creative Commons Attribution (http://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Articles
Bradshaw, William J.
Kirby, Jonathan M.
Roberts, April K.
Shone, Clifford C.
Acharya, K. Ravi
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title_full The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title_fullStr The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title_full_unstemmed The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title_short The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
title_sort molecular structure of the glycoside hydrolase domain of cwp19 from clostridium difficile
topic Original Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5765458/
https://www.ncbi.nlm.nih.gov/pubmed/29083543
http://dx.doi.org/10.1111/febs.14310
work_keys_str_mv AT bradshawwilliamj themolecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT kirbyjonathanm themolecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT robertsaprilk themolecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT shonecliffordc themolecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT acharyakravi themolecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT bradshawwilliamj molecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT kirbyjonathanm molecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT robertsaprilk molecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT shonecliffordc molecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile
AT acharyakravi molecularstructureoftheglycosidehydrolasedomainofcwp19fromclostridiumdifficile