Home > Publications database > SbsB structure and lattice reconstruction unveil $\mathrm{Ca^{2^+}}$ triggered S-layer assembly > print

001     142539
005     20250730162640.0
024 7 _ |2 pmid
|a pmid:22722836
024 7 _ |2 ISSN
|a 1476-4687
024 7 _ |2 ISSN
|a 0028-0836
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|a WOS:000305982900062
024 7 _ |2 doi
|a 10.1038/nature11155
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037 _ _ |a PHPPUBDB-25515
041 _ _ |a English
082 _ _ |a 070
100 1 _ |a Baranova, E.
|b 0
110 1 _ |a DESY
|b European Molecular Biology Laboratory
245 _ _ |a SbsB structure and lattice reconstruction unveil $\mathrm{Ca^{2^+}}$ triggered S-layer assembly
260 _ _ |a London [u.a.]
|b Nature Publ. Group
|c 2012
300 _ _ |a 119-122
336 7 _ |2 DRIVER
|a article
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|a Output Types/Journal article
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|a Journal Article
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|s 1519381701_18001
336 7 _ |2 BibTeX
|a ARTICLE
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|a JOURNAL_ARTICLE
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|2 EndNote
|a Journal Article
440 _ 0 |0 PERI:(DE-600)1413423-8
|a Nature
|v 487
|x 0028-0836
|y 7405
500 _ _ |3 Converted on 2013-05-30 09:57
500 _ _ |3 Converted on 2013-06-21 19:21
520 _ _ |a 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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|c POF2-54G13
|a DORIS Beamline D1.2 (POF2-54G13)
588 _ _ |a Dataset connected to Pubmed
650 _ 7 |0 0
|2 NLM Chemicals
|a Bacterial Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a Immunoglobulins
650 _ 7 |0 0
|2 NLM Chemicals
|a Membrane Proteins
650 _ 7 |0 0
|2 NLM Chemicals
|a SbsB protein, Bacillus stearothermophilus
650 _ 7 |0 0
|2 NLM Chemicals
|a Solutions
650 _ 7 |0 7440-70-2
|2 NLM Chemicals
|a Calcium
650 _ 2 |2 MeSH
|a Bacterial Proteins: chemistry
650 _ 2 |2 MeSH
|a Bacterial Proteins: metabolism
650 _ 2 |2 MeSH
|a Calcium: chemistry
650 _ 2 |2 MeSH
|a Calcium: metabolism
650 _ 2 |2 MeSH
|a Calcium: pharmacology
650 _ 2 |2 MeSH
|a Cryoelectron Microscopy
650 _ 2 |2 MeSH
|a Crystallization: methods
650 _ 2 |2 MeSH
|a Crystallography, X-Ray
650 _ 2 |2 MeSH
|a Geobacillus stearothermophilus: chemistry
650 _ 2 |2 MeSH
|a Immunoglobulins: chemistry
650 _ 2 |2 MeSH
|a Membrane Proteins: chemistry
650 _ 2 |2 MeSH
|a Membrane Proteins: metabolism
650 _ 2 |2 MeSH
|a Models, Molecular
650 _ 2 |2 MeSH
|a Molecular Dynamics Simulation
650 _ 2 |2 MeSH
|a Nanostructures: chemistry
650 _ 2 |2 MeSH
|a Polymerization: drug effects
650 _ 2 |2 MeSH
|a Protein Structure, Quaternary: drug effects
650 _ 2 |2 MeSH
|a Protein Structure, Tertiary: drug effects
650 _ 2 |2 MeSH
|a Solutions
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700 1 _ |a Fronzes, R.
|b 1
700 1 _ |a Garcia-Pino, A.
|b 2
700 1 _ |a Van Gerven, N.
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700 1 _ |a Papapostolou, D.
|b 4
700 1 _ |a Pehau-Arnaudet, G.
|b 5
700 1 _ |a Pardon, E.
|b 6
700 1 _ |a Steyaert, J.
|b 7
700 1 _ |a Howorka, S.
|b 8
700 1 _ |0 P:(DE-HGF)0
|a Remaut, H.
|b 9
|e Corresponding author
773 _ _ |0 PERI:(DE-600)1413423-8
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