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Publication Detail
SbsB structure and lattice reconstruction unveil Ca2+ triggered S-layer assembly.
  • Publication Type:
    Journal article
  • Publication Sub Type:
    Journal Article
  • Authors:
    Baranova E, Fronzes R, Garcia-Pino A, Van Gerven N, Papapostolou D, Péhau-Arnaudet G, Pardon E, Steyaert J, Howorka S, Remaut H
  • Publication date:
    05/07/2012
  • Pagination:
    119, 122
  • Journal:
    Nature
  • Volume:
    487
  • Issue:
    7405
  • Country:
    England
  • PII:
    nature11155
  • Language:
    eng
  • Keywords:
    Bacterial Proteins, Calcium, Cryoelectron Microscopy, Crystallization, Crystallography, X-Ray, Geobacillus stearothermophilus, Immunoglobulins, Membrane Proteins, Models, Molecular, Molecular Dynamics Simulation, Nanostructures, Polymerization, Protein Structure, Quaternary, Protein Structure, Tertiary, Solutions
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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