ArticleIUCrJ2016
Peptide binding to a bacterial signal peptidase visualized by peptide tethering and carrier-driven crystallization.
Article in IUCrJ, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 23 citations in OpenAlex.
- Structural basis of signal peptide recognition by the signal peptidase complex.Nature communications · 2026Article
- The Role of the Omega Subzone in Determining the Membership of a Protein in One of the Two Families of the LexA/Signal Peptidase-like Superfamily.International journal of molecular sciences · 2026Article
- Dynamic nature of Staphylococcus aureus type I signal peptidases.Biophysical journal · 2025Article
- Article
- Signal peptidase SpsB coordinates staphylococcal cell cycle, surface protein septal trafficking and LTA synthesis.bioRxiv : the preprint server for biology · 2024Article
- Unraveling the mechanism of small molecule induced activation of Staphylococcus aureus signal peptidase IB.Communications biology · 2024Article
- Increasing the Efficiency of the Accumulation of Recombinant Proteins in Plant Cells: The Role of Transport Signal Peptides.Plants (Basel, Switzerland) · 2022Review
- Antimicrobial Activity of Rhenium Di- and Tricarbonyl Diimine Complexes: Insights on Membrane-BoundPharmaceuticals (Basel, Switzerland) · 2022Article
- Targeted Isolation of Antibiotic Brominated Alkaloids from the Marine SpongeMarine drugs · 2022Article
- Bacterial Signal Peptides- Navigating the Journey of Proteins.Frontiers in physiology · 2022Review
- Emerging peptide antibiotics with therapeutic potential.Medicine in drug discovery · 2021Review
- Group AInfection and immunity · 2019Article
- Review
- Protein export through the bacterial Sec pathway.Nature reviews. Microbiology · 2017Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial type I signal peptidases (SPases) are membrane-anchored serine proteases that process the signal peptides of proteins exported via the Sec and Tat secretion systems. Despite their crucial importance for bacterial virulence and their attractiveness as drug targets, only one such enzyme, LepB from Escherichia coli, has been structurally characterized, and the transient nature of peptide binding has stymied attempts to directly visualize SPase-substrate complexes. Here, the crystal structure of SpsB, the type I signal peptidase from the Gram-positive pathogen Staphylococcus aureus, is reported, and a peptide-tethering strategy that exploits the use of carrier-driven crystallization is described. This enabled the determination of the crystal structures of three SpsB-peptide complexes, both with cleavable substrates and with an inhibitory peptide. SpsB-peptide interactions in these complexes are almost exclusively limited to the canonical signal-peptide motif Ala-X-Ala, for which clear specificity pockets are found. Minimal contacts are made outside this core, with the variable side chains of the peptides accommodated in shallow grooves or exposed faces. These results illustrate how high fidelity is retained despite broad sequence diversity, in a process that is vital for cell survival.
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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.