ArticleThe FEBS journal2017
The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.
Article in The FEBS journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- A Cold-Induced LEA3 Protein, DohD, Confers Cryoprotective Protection Against Low-Temperature Stress inInternational journal of molecular sciences · 2025Article
- A Novel Glycoside Hydrolase DogH Utilizing Soluble Starch to Maltose Improve Osmotic Tolerance inInternational journal of molecular sciences · 2023Article
- Host Immune Responses to Surface S-Layer Proteins (SLPs) ofMicroorganisms · 2023Review
- Design and characterization of a novel lytic protein against Clostridium difficile.Applied microbiology and biotechnology · 2022Article
- TheMicrobiology spectrum · 2022Article
- Predictive regulatory and metabolic network models for systems analysis of Clostridioides difficile.Cell host & microbe · 2021Article
- The Tol-Pal system is required for peptidoglycan-cleaving enzymes to complete bacterial cell division.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Inverting family GH156 sialidases define an unusual catalytic motif for glycosidase action.Nature communications · 2019Article
- The Two Distinct Types of SecA2-Dependent Export Systems.Microbiology spectrum · 2019Review
- Article
- The structure of the S-layer of Clostridium difficile.Journal of cell communication and signaling · 2018Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
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. DATABASE: Structural data are available in the PDB under the accession numbers 5OQ2 and 5OQ3.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.