ArticleProtein science : a publication of the Protein Society2022
Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.
Article in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 5 citations in OpenAlex.
- An Investigation of the Conformational Dynamics of ABC Exporter PCAT1 using Microsecond-Level MD Simulations.bioRxiv : the preprint server for biology · 2026Article
- The Microbial Anti-Inflammatory Molecule (MAM) is a key protein processed and exported toGut microbes · 2025Article
- Type 1 secretion necessitates a tight interplay between all domains of the ABC transporter.Scientific reports · 2024Article
- Proteases Involved in Leader Peptide Removal during RiPP Biosynthesis.ACS bio & med chem Au · 2024Review
- Structural and dynamic studies of the peptidase domain from Clostridium thermocellum PCAT1.Protein science : a publication of the Protein Society · 2022Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The export of antimicrobial peptides is mediated by diverse mechanisms in bacterial quorum sensing pathways. One such binary system employed by gram-positive bacteria is the PCAT1 ABC transporter coupled to a cysteine protease. The focus of this study is the N-terminal C39 peptidase (PEP) domain from Clostridium thermocellum PCAT1 that processes its natural substrate CtA by cleaving a conserved -GG- motif to separate the cargo from the leader peptide prior to secretion. In this study, we are primarily interested in elucidating the dynamic and structural determinants of CtA binding and how it is coupled to cleavage efficiency in the PCAT1 PEP domain. To this end, we have characterized CtA interactions with PEP domain and PCAT1 transporter in detergent micelles using solution nuclear magnetic resonance spectroscopy. The bound CtA structure revealed the disordered C-terminal cargo peptide is linked by a sterically hindered cleavage site to a helix docked within a hydrophobic cavity in the PEP domain. The wide range of internal motions detected by amide nitrogen (N
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Registered trials
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