ArticleActa crystallographica. Section D, Biological crystallography2014
The structure of the cysteine protease and lectin-like domains of Cwp84, a surface layer-associated protein from Clostridium difficile.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Conformational changes of the baseplate regulating tail contraction of Staphylococcus phage 812.The EMBO journal · 2026Article
- Origin and Early Diversification of the Papain Family of Cysteine Peptidases.International journal of molecular sciences · 2023Article
- Detection of Newly Secreted Antibodies Predicts Nonrecurrence in Primary Clostridioides difficile Infection.Journal of clinical microbiology · 2022Article
- The structure of the S-layer of Clostridium difficile.Journal of cell communication and signaling · 2018Review
- The molecular structure of the glycoside hydrolase domain of Cwp19 from Clostridium difficile.The FEBS journal · 2017Article
- Cwp2 from Clostridium difficile exhibits an extended three domain fold and cell adhesion in vitro.The FEBS journal · 2017Article
- Computational investigation of conformational variability and allostery in cathepsin K and other related peptidases.PloS one · 2017Article
- An update on antibody-based immunotherapies for Clostridium difficile infection.Clinical and experimental gastroenterology · 2016Review
- Cwp84, a Clostridium difficile cysteine protease, exhibits conformational flexibility in the absence of its propeptide.Acta crystallographica. Section F, Structural biology communications · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Clostridium difficile is a major problem as an aetiological agent for antibiotic-associated diarrhoea. The mechanism by which the bacterium colonizes the gut during infection is poorly understood, but undoubtedly involves a myriad of components present on the bacterial surface. The mechanism of C. difficile surface-layer (S-layer) biogenesis is also largely unknown but involves the post-translational cleavage of a single polypeptide (surface-layer protein A; SlpA) into low- and high-molecular-weight subunits by Cwp84, a surface-located cysteine protease. Here, the first crystal structure of the surface protein Cwp84 is described at 1.4 Å resolution and the key structural components are identified. The truncated Cwp84 active-site mutant (amino-acid residues 33-497; C116A) exhibits three regions: a cleavable propeptide and a cysteine protease domain which exhibits a cathepsin L-like fold followed by a newly identified putative carbohydrate-binding domain with a bound calcium ion, which is referred to here as a lectin-like domain. This study thus provides the first structural insights into Cwp84 and a strong base to elucidate its role in the C. difficile S-layer maturation mechanism.
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