Journal
NATURE
Volume 487, Issue 7405, Pages 119-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature11155
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Funding
- VIB (Vlaams Institute voor Biotechnologie) [PRJ9]
- Fonds Wetenschappelijk Onderzoek-Vlaanderen through an Odysseus grant
- Centre National de la Recherche Scientifique (CNRS)
- Institut Pasteur
- Interuniversity Attraction Poles grant [P6/19]
- Biotechnology and Biological Sciences Research Council [BB/E010466/1]
- University College London
- [FWO551]
- BBSRC [BB/E010466/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E010466/1] Funding Source: researchfish
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S-layers are regular two-dimensional semipermeable protein layers that constitute a major cell-wall component in archaea and many bacteria(1-3). 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(4-7). Despite their biological abundance and the technological interest in them, structural information about SLPs is limited to truncated and assembly-negative proteins(8-10). 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 phi-shaped disk-like monomeric crystallization unit stabilized by interdomain Ca2+ ion coordination. A Ca2+-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(4-7).
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