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@ARTICLE{Baranova:142539,
author = {Baranova, E. and Fronzes, R. and Garcia-Pino, A. and Van
Gerven, N. and Papapostolou, D. and Pehau-Arnaudet, G. and
Pardon, E. and Steyaert, J. and Howorka, S. and Remaut, H.
and DESY},
title = {{S}bs{B} structure and lattice reconstruction unveil
$\mathrm{{C}a^{2^+}}$ triggered {S}-layer assembly},
journal = {Nature},
volume = {487},
issn = {0028-0836},
address = {London [u.a.]},
publisher = {Nature Publ. Group},
reportid = {PHPPUBDB-25515},
pages = {119 - 122},
year = {2012},
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.},
keywords = {Bacterial Proteins: chemistry / Bacterial Proteins:
metabolism / Calcium: chemistry / Calcium: metabolism /
Calcium: pharmacology / Cryoelectron Microscopy /
Crystallization: methods / Crystallography, X-Ray /
Geobacillus stearothermophilus: chemistry / Immunoglobulins:
chemistry / Membrane Proteins: chemistry / Membrane
Proteins: metabolism / Models, Molecular / Molecular
Dynamics Simulation / Nanostructures: chemistry /
Polymerization: drug effects / Protein Structure,
Quaternary: drug effects / Protein Structure, Tertiary: drug
effects / Solutions / Bacterial Proteins (NLM Chemicals) /
Immunoglobulins (NLM Chemicals) / Membrane Proteins (NLM
Chemicals) / SbsB protein, Bacillus stearothermophilus (NLM
Chemicals) / Solutions (NLM Chemicals) / Calcium (NLM
Chemicals)},
cin = {EMBL(-2012)},
ddc = {070},
cid = {$I:(DE-H253)EMBL_-2012_-20130307$},
pnm = {DORIS Beamline D1.2 (POF2-54G13)},
pid = {G:(DE-H253)POF2-D1.2-20130405},
experiment = {EXP:(DE-H253)D-D1.2-20150101},
typ = {PUB:(DE-HGF)16},
pubmed = {pmid:22722836},
UT = {WOS:000305982900062},
doi = {10.1038/nature11155},
url = {https://bib-pubdb1.desy.de/record/142539},
}