Journal Article

PHPPUBDB-25515

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png SbsB structure and lattice reconstruction unveil $\mathrm{Ca^{2^+}}$ triggered S-layer assembly

Baranova, E. ; Fronzes, R. ; Garcia-Pino, A. ; Van Gerven, N. ; Papapostolou, D. ; Pehau-Arnaudet, G. ; Pardon, E. ; Steyaert, J. ; Howorka, S. ; Remaut, H. (Corresponding author) ; DESY

2012
Nature Publ. Group London [u.a.]

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Please use a persistent id in citations: doi:10.1038/nature11155

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.

Keyword(s): Bacterial Proteins: chemistry (MeSH) ; Bacterial Proteins: metabolism (MeSH) ; Calcium: chemistry (MeSH) ; Calcium: metabolism (MeSH) ; Calcium: pharmacology (MeSH) ; Cryoelectron Microscopy (MeSH) ; Crystallization: methods (MeSH) ; Crystallography, X-Ray (MeSH) ; Geobacillus stearothermophilus: chemistry (MeSH) ; Immunoglobulins: chemistry (MeSH) ; Membrane Proteins: chemistry (MeSH) ; Membrane Proteins: metabolism (MeSH) ; Models, Molecular (MeSH) ; Molecular Dynamics Simulation (MeSH) ; Nanostructures: chemistry (MeSH) ; Polymerization: drug effects (MeSH) ; Protein Structure, Quaternary: drug effects (MeSH) ; Protein Structure, Tertiary: drug effects (MeSH) ; Solutions (MeSH) ; Bacterial Proteins ; Immunoglobulins ; Membrane Proteins ; SbsB protein, Bacillus stearothermophilus ; Solutions ; Calcium

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Contributing Institute(s):

1. EMBL (EMBL(-2012))

Research Program(s):

1. DORIS Beamline D1.2 (POF2-54G13) (POF2-54G13)

Experiment(s):

1. DORIS Beamline D1.2 (DORIS III)

Appears in the scientific report 2012

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Database coverage:
; BIOSIS Previews ; Current Contents - Agriculture, Biology and Environmental Sciences ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; Ebsco Academic Search ; IF >= 30 ; JCR ; NCBI Molecular Biology Database ; Nationallizenz ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection ; Zoological Record

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