ArticlePLoS genetics2021
A lipoprotein allosterically activates the CwlD amidase during Clostridioides difficile spore formation.
Article in PLoS genetics, 2021. 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, 17 citations in OpenAlex.
- Structure of core assembly of the Clostridioides difficile germinosome.Nature communications · 2026Article
- Targeting SleC and CspB in the Inhibition of Spore Germination inJournal of medicinal chemistry · 2025Article
- Reactions of SleC, Its Structure and Inhibition in Mitigation of Spore Germination inJournal of the American Chemical Society · 2025Article
- Bile acids as germinants for Clostridioides difficile spores, evidence of adaptation to the gut?FEMS microbiology reviews · 2025Review
- Bioinformatic and experimental identification and characterization ofFrontiers in immunology · 2025Article
- Metalation of Extracytoplasmic Proteins and Bacterial Cell Envelope Homeostasis.Annual review of microbiology · 2024Review
- The small acid-soluble proteins of Clostridioides difficile regulate sporulation in a SpoIVB2-dependent manner.PLoS pathogens · 2024Article
- The small acid-soluble proteins ofbioRxiv : the preprint server for biology · 2024Article
- Clostridioides difficile Sporulation.Advances in experimental medicine and biology · 2024Review
- Reconstituting Spore Cortex Peptidoglycan Biosynthesis Reveals a Deacetylase That Catalyzes Transamidation.Biochemistry · 2023Article
- Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Spore-forming pathogens like Clostridioides difficile depend on germination to initiate infection. During gemination, spores must degrade their cortex layer, which is a thick, protective layer of modified peptidoglycan. Cortex degradation depends on the presence of the spore-specific peptidoglycan modification, muramic-∂-lactam (MAL), which is specifically recognized by cortex lytic enzymes. In C. difficile, MAL production depends on the CwlD amidase and its binding partner, the GerS lipoprotein. To gain insight into how GerS regulates CwlD activity, we solved the crystal structure of the CwlD:GerS complex. In this structure, a GerS homodimer is bound to two CwlD monomers such that the CwlD active sites are exposed. Although CwlD structurally resembles amidase_3 family members, we found that CwlD does not bind Zn2+ stably on its own, unlike previously characterized amidase_3 enzymes. Instead, GerS binding to CwlD promotes CwlD binding to Zn2+, which is required for its catalytic mechanism. Thus, in determining the first structure of an amidase bound to its regulator, we reveal stabilization of Zn2+ co-factor binding as a novel mechanism for regulating bacterial amidase activity. Our results further suggest that allosteric regulation by binding partners may be a more widespread mode for regulating bacterial amidase activity than previously thought.
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