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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...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2017
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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 |
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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
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title_full | The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
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title_fullStr | The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
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title_full_unstemmed | The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
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title_short | The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile
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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 |
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