ArticleThe Journal of biological chemistry2011
Structure of surface layer homology (SLH) domains from Bacillus anthracis surface array protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 86 citations in OpenAlex.
- Phylogeny constrains and environment modulates glycoside hydrolase architecture.Current research in microbial sciences · 2026Article
- Self-assembly of surface layer protein SbsC from Geobacillus stearothermophilus and common principles of Bacilli S-layers.The Journal of biological chemistry · 2026Article
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Enzymatic property and stabilization mechanism of LysBT1, a novel polyextremotolerant endolysin with a C-terminal S-layer homology domain.Applied and environmental microbiology · 2025Article
- Crystal structure of the C1 domain of the surface-layer protein SlpM from Lactobacillus brevis: a module involved in protein self-assembly.Acta crystallographica. Section F, Structural biology communications · 2025Article
- A new age in structural S-layer biology: Experimental and in silico milestones.The Journal of biological chemistry · 2025Review
- Molecular dynamics and machine learning stratify motion-dependent activity profiles of S-layer destabilizing nanobodies.PNAS nexus · 2024Article
- Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes.Nature communications · 2023Article
- Molecular modelling and site-directed mutagenesis provide insight into saccharide pyruvylation by the Paenibacillus alvei CsaB enzyme.Scientific reports · 2023Article
- Engineering Caldicellulosiruptor bescii with Surface Layer Homology Domain-Linked Glycoside Hydrolases Improves Plant Biomass Solubilization.Applied and environmental microbiology · 2022Article
- A multidomain connector links the outer membrane and cell wall in phylogenetically deep-branching bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structure and assembly of the S-layer in C. difficile.Nature communications · 2022Article
- Dynamic Profile of S-Layer Proteins Controls Surface Properties of EmeticFrontiers in microbiology · 2022Article
- Phylogenetic analysis of the bacterial Pro-Pro-endopeptidase domain reveals a diverse family including secreted and membrane anchored proteins.Current research in microbial sciences · 2021Review
- Molecular Logic of Prokaryotic Surface Layer Structures.Trends in microbiology · 2021Review
- S-layers: The Proteinaceous Multifunctional Armors of Gram-Positive Pathogens.Frontiers in microbiology · 2021Review
- TheMicroorganisms · 2020Review
- Structural insights into the main S-layer unit ofThe Journal of biological chemistry · 2020Article
- Structure of S-layer protein Sap reveals a mechanism for therapeutic intervention in anthrax.Nature microbiology · 2019Article
- Pyruvate Substitutions on Glycoconjugates.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Surface (S)-layers, para-crystalline arrays of protein, are deposited in the envelope of most bacterial species. These surface organelles are retained in the bacterial envelope through the non-covalent association of proteins with cell wall carbohydrates. Bacillus anthracis, a Gram-positive pathogen, produces S-layers of the protein Sap, which uses three consecutive repeats of the surface-layer homology (SLH) domain to engage secondary cell wall polysaccharides (SCWP). Using x-ray crystallography, we reveal here the structure of these SLH domains, which assume the shape of a three-prong spindle. Each SLH domain contributes to a three-helical bundle at the spindle base, whereas another α-helix and its connecting loops generate the three prongs. The inter-prong grooves contain conserved cationic and anionic residues, which are necessary for SLH domains to bind the B. anthracis SCWP. Modeling experiments suggest that the SLH domains of other S-layer proteins also fold into three-prong spindles and capture bacterial envelope carbohydrates by a similar mechanism.
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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.