ArticleeLife2019
Insights into AMS/PCAT transporters from biochemical and structural characterization of a double Glycine motif protease.
Article in eLife, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
69 citing papers in PubMed, 92 citations in OpenAlex.
- Exploring RiPP-derivedRSC chemical biology · 2026Article
- Diversity and Classification of the Actinopeptins: A New Family of Lanthipeptides Within the Genomes from the Phylum Actinomycetota.Antibiotics (Basel, Switzerland) · 2026Article
- Structure and Activity of Class II Lanthipeptides From a Thermophilic Bacterium.Chembiochem : a European journal of chemical biology · 2026Article
- TMcin RiPP biosynthesis in the cellular membrane.bioRxiv : the preprint server for biology · 2026Article
- Structure and Activity of Class II Lanthipeptides from a Thermophilic Bacterium.bioRxiv : the preprint server for biology · 2026Article
- Structure, Biosynthesis, and Bioactivity of Nostolysamides.Biochemistry · 2026Article
- Structure, biosynthesis, and bioactivity of nostolysamides.bioRxiv : the preprint server for biology · 2026Article
- An Unusual Ring Pattern in the Rosβ Lanthipeptide of the Two-Component Lantibiotic Roseocin.Journal of natural products · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme during RiPP Biosynthesis.Journal of the American Chemical Society · 2026Article
- Oxidative Peptide Backbone Cleavage by a HEXXH Enzyme During RiPP Biosynthesis.bioRxiv : the preprint server for biology · 2025Article
- Peptide Prenylation Follows Divergent Substrate Engagement Rules.Journal of the American Chemical Society · 2025Article
- The Microbial Anti-Inflammatory Molecule (MAM) is a key protein processed and exported toGut microbes · 2025Article
- Large protein-like leader peptides engage differently with RiPP halogenases and lanthionine synthetases.Nature communications · 2025Article
- Promiscuity of lanthipeptide enzymes: new challenges and applications.World journal of microbiology & biotechnology · 2025Review
- Antibacterial microcins are ubiquitous and functionally diverse across bacterial communities.Nature communications · 2025Article
- Discovery of a Two-Step Enzyme Cascade Converting Aspartate to Aminomalonate in Peptide Natural Product Biosynthesis.Journal of the American Chemical Society · 2025Article
- Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025Article
- Design and Production of Geranylated Cyclic Peptides by the RiPP Enzymes SyncM and PirF.Biomacromolecules · 2025Article
- An interbacterial cysteine protease toxin inhibits cell growth by targeting type II DNA topoisomerases GyrB and ParE.PLoS biology · 2025Article
- De novo design of ribosomally synthesized and post-translationally modified peptides.Nature chemistry · 2025Article
9 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The secretion of peptides and proteins is essential for survival and ecological adaptation of bacteria. Dual-functional ATP-binding cassette transporters export antimicrobial or quorum signaling peptides in Gram-positive bacteria. Their substrates contain a leader sequence that is excised by an N-terminal peptidase C39 domain at a double Gly motif. We characterized the protease domain (LahT150) of a transporter from a lanthipeptide biosynthetic operon in Lachnospiraceae and demonstrate that this protease can remove the leader peptide from a diverse set of peptides. The 2.0 Å resolution crystal structure of the protease domain in complex with a covalently bound leader peptide demonstrates the basis for substrate recognition across the entire class of such transporters. The structural data also provide a model for understanding the role of leader peptide recognition in the translocation cycle, and the function of degenerate, non-functional C39-like domains (CLD) in substrate recruitment in toxin exporters in Gram-negative bacteria.
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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.