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@ARTICLE{VanderMeeren:141270,
      author       = {Van der Meeren, R. and Wen, Y. and Van Gelder, P. and
                      Tommassen, J. and Devreese, B. and Savvides, S. N. and DESY},
      title        = {{N}ew insights into the assembly of bacterial secretins:
                      structural studies of the periplasmic domain of {X}cp{Q}
                      from {P}seudomonas aeruginosa},
      journal      = {The journal of biological chemistry},
      volume       = {288},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {PHPPUBDB-25356},
      pages        = {1214-1225},
      year         = {2013},
      abstract     = {The type II secretion system is a multiprotein assembly
                      spanning the inner and outer membranes in Gram-negative
                      bacteria. It is found in almost all pathogenic bacteria
                      where it contributes to virulence, host tissue colonization,
                      and infection. The exoproteins are secreted across the outer
                      membrane via a large translocation channel, the secretin,
                      which typically adopts a dodecameric structure. These
                      secretin channels have large periplasmic N-terminal domains
                      that reach out into the periplasm for communication with the
                      inner membrane platform and with a pseudopilus structure
                      that spans the periplasm. Here we report the crystal
                      structure of the N-terminal periplasmic domain of the
                      secretin XcpQ from Pseudomonas aeruginosa, revealing a
                      two-lobe dimeric assembly featuring parallel subunits
                      engaging in well defined interactions at the tips of each
                      lobe. We have employed structure-based engineering of
                      disulfide bridges and native mass spectrometry to show that
                      the periplasmic domain of XcpQ dimerizes in a
                      concentration-dependent manner. Validation of these insights
                      in the context of cellular full-length XcpQ and further
                      evaluation of the functionality of disulfide-linked XcpQ
                      establishes that the basic oligomerization unit of XcpQ is a
                      dimer. This is consistent with the notion that the
                      dodecameric secretin assembles as a hexamer of dimers to
                      ensure correct projection of the N-terminal domains into the
                      periplasm. Therefore, our studies provide a key conceptual
                      advancement in understanding the assembly principles and
                      dynamic function of type II secretion system secretins and
                      challenge recent studies reporting monomers as the basic
                      subunit of the secretin oligomer.},
      keywords     = {Amino Acid Sequence / Bacterial Proteins: chemistry /
                      Bacterial Proteins: genetics / Bacterial Proteins:
                      metabolism / Electrophoresis, Polyacrylamide Gel / Mass
                      Spectrometry / Molecular Sequence Data / Periplasm:
                      metabolism / Protein Conformation / Pseudomonas aeruginosa:
                      metabolism / Recombinant Proteins: chemistry / Recombinant
                      Proteins: genetics / Recombinant Proteins: metabolism /
                      Secretin: metabolism / Sequence Homology, Amino Acid /
                      Bacterial Proteins (NLM Chemicals) / Recombinant Proteins
                      (NLM Chemicals) / Secretin (NLM Chemicals)},
      cin          = {EMBL},
      ddc          = {570},
      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:23188826},
      pmc          = {pmc:PMC3543004},
      UT           = {WOS:000313570300042},
      doi          = {10.1074/jbc.M112.432096},
      url          = {https://bib-pubdb1.desy.de/record/141270},
}