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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},
}