ArticleNature2012
SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly.
Article in Nature, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.
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Who cites it
77 citing papers in PubMed.
- Free-standing ultrathin two-dimensional peptide crystals.Nature chemistry · 2026Article
- Self-assembly of surface layer protein SbsC from Geobacillus stearothermophilus and common principles of Bacilli S-layers.The Journal of biological chemistry · 2026Article
- The calcium signal regulatory network and the roles of calcium-binding proteins in bacteria.World journal of microbiology & biotechnology · 2026Review
- Nanobody-mediated control of long RSH Rel and RelA catalysis by restriction of their conformational landscape.Nature communications · 2026Article
- Assembly, architecture and functional roles of microbial surface layers.Nature reviews. Microbiology · 2026Review
- Donor strand complementation and calcium ion coordination drive the chaperone-free polymerization of archaeal cannulae.Nature communications · 2025Article
- Cryo-EM structure and polar assembly of the PS2 S-layer ofProceedings of the National Academy of Sciences of the United States of America · 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
- Sandwiching of MOF nanoparticles between graphene oxide nanosheets among ice grains.Nature communications · 2025Article
- Mapping the ultrastructural topology of the corynebacterial cell surface.PLoS biology · 2025Article
- Assembly and Functionality of 2D Protein Arrays.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Review
- Architecture of the Sap S-layer ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Composition and in situ structure of theScience advances · 2024Article
- Molecular dynamics and machine learning stratify motion-dependent activity profiles of S-layer destabilizing nanobodies.PNAS nexus · 2024Article
- Article
- Cell cycle dependent coordination of surface layer biogenesis in Caulobacter crescentus.Nature communications · 2024Article
- A nanobody inhibitor of Fascin-1 actin-bundling activity and filopodia formation.Open biology · 2024Article
- Structural characterization and functional insights into the type II secretion system of the poly-extremophile Deinococcus radiodurans.The Journal of biological chemistry · 2024Article
- Article
17 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
S-layers are regular two-dimensional semipermeable protein layers that constitute a major cell-wall component in archaea and many bacteria. The nanoscale repeat structure of the S-layer lattices and their self-assembly from S-layer proteins (SLPs) have sparked interest in their use as patterning and display scaffolds for a range of nano-biotechnological applications. Despite their biological abundance and the technological interest in them, structural information about SLPs is limited to truncated and assembly-negative proteins. Here we report the X-ray structure of the SbsB SLP of Geobacillus stearothermophilus PV72/p2 by the use of nanobody-aided crystallization. SbsB consists of a seven-domain protein, formed by an amino-terminal cell-wall attachment domain and six consecutive immunoglobulin-like domains, that organize into a φ-shaped disk-like monomeric crystallization unit stabilized by interdomain Ca(2+) ion coordination. A Ca(2+)-dependent switch to the condensed SbsB quaternary structure pre-positions intermolecular contact zones and renders the protein competent for S-layer assembly. On the basis of crystal packing, chemical crosslinking data and cryo-electron microscopy projections, we present a model for the molecular organization of this SLP into a porous protein sheet inside the S-layer. The SbsB lattice represents a previously undescribed structural model for protein assemblies and may advance our understanding of SLP physiology and self-assembly, as well as the rational design of engineered higher-order structures for biotechnology.
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Registered trials
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