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000142539 1001_ $$aBaranova, E.$$b0
000142539 1101_ $$aDESY$$bEuropean Molecular Biology Laboratory
000142539 245__ $$aSbsB structure and lattice reconstruction unveil $\mathrm{Ca^{2^+}}$ triggered S-layer assembly
000142539 260__ $$aLondon [u.a.]$$bNature Publ. Group$$c2012
000142539 300__ $$a119-122
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000142539 440_0 $$0PERI:(DE-600)1413423-8$$aNature$$v487$$x0028-0836$$y7405
000142539 500__ $$3Converted on 2013-05-30 09:57
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000142539 520__ $$aS-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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000142539 650_7 $$00$$2NLM Chemicals$$aBacterial Proteins
000142539 650_7 $$00$$2NLM Chemicals$$aImmunoglobulins
000142539 650_7 $$00$$2NLM Chemicals$$aMembrane Proteins
000142539 650_7 $$00$$2NLM Chemicals$$aSbsB protein, Bacillus stearothermophilus
000142539 650_7 $$00$$2NLM Chemicals$$aSolutions
000142539 650_7 $$07440-70-2$$2NLM Chemicals$$aCalcium
000142539 650_2 $$2MeSH$$aBacterial Proteins: chemistry
000142539 650_2 $$2MeSH$$aBacterial Proteins: metabolism
000142539 650_2 $$2MeSH$$aCalcium: chemistry
000142539 650_2 $$2MeSH$$aCalcium: metabolism
000142539 650_2 $$2MeSH$$aCalcium: pharmacology
000142539 650_2 $$2MeSH$$aCryoelectron Microscopy
000142539 650_2 $$2MeSH$$aCrystallization: methods
000142539 650_2 $$2MeSH$$aCrystallography, X-Ray
000142539 650_2 $$2MeSH$$aGeobacillus stearothermophilus: chemistry
000142539 650_2 $$2MeSH$$aImmunoglobulins: chemistry
000142539 650_2 $$2MeSH$$aMembrane Proteins: chemistry
000142539 650_2 $$2MeSH$$aMembrane Proteins: metabolism
000142539 650_2 $$2MeSH$$aModels, Molecular
000142539 650_2 $$2MeSH$$aMolecular Dynamics Simulation
000142539 650_2 $$2MeSH$$aNanostructures: chemistry
000142539 650_2 $$2MeSH$$aPolymerization: drug effects
000142539 650_2 $$2MeSH$$aProtein Structure, Quaternary: drug effects
000142539 650_2 $$2MeSH$$aProtein Structure, Tertiary: drug effects
000142539 650_2 $$2MeSH$$aSolutions
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000142539 7001_ $$aFronzes, R.$$b1
000142539 7001_ $$aGarcia-Pino, A.$$b2
000142539 7001_ $$aVan Gerven, N.$$b3
000142539 7001_ $$aPapapostolou, D.$$b4
000142539 7001_ $$aPehau-Arnaudet, G.$$b5
000142539 7001_ $$aPardon, E.$$b6
000142539 7001_ $$aSteyaert, J.$$b7
000142539 7001_ $$aHoworka, S.$$b8
000142539 7001_ $$0P:(DE-HGF)0$$aRemaut, H.$$b9$$eCorresponding author
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