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@ARTICLE{Merilinen:321838,
      author       = {Meriläinen, Gitte and Koski, M. Kristian and Wierenga, Rik
                      K.},
      title        = {{T}he extended structure of the periplasmic region of
                      {C}ds{D}, a structural protein of the type {III} secretion
                      system of {C}hlamydia trachomatis},
      journal      = {Protein science},
      volume       = {25},
      number       = {5},
      issn         = {0961-8368},
      address      = {Hoboken, NJ},
      publisher    = {Wiley},
      reportid     = {PUBDB-2017-02769},
      pages        = {987 - 998},
      year         = {2016},
      abstract     = {The type III secretion system (T3SS) is required for the
                      virulence of many gram-negative bacterial human pathogens.
                      It is composed of several structural proteins, forming the
                      secretion needle and its basis, the basal body. In Chlamydia
                      spp., the T3SS inner membrane ring (IM-ring) of the basal
                      body is formed by the periplasmic part of CdsD (outer ring)
                      and CdsJ (inner ring). Here we describe the crystal
                      structure of the C-terminal, periplasmic part of CdsD, not
                      including the last 60 residues. Two crystal forms were
                      obtained, grown in three different crystallization
                      conditions. In both crystal forms there is one molecule per
                      asymmetric unit adopting a similar extended structure. The
                      structures consist of three periplasmic domains (PDs) of
                      similar αββαβ topology as seen also in the structures
                      of the homologous PrgH (Salmonella typhimurium) and YscD
                      (Yersinia enterocolitica). Only in the C2 crystal form,
                      there is a C-terminal additional helix after the PD3 domain.
                      The relative orientation of the three subsequent CdsD PD
                      domains with respect to each other is more extended than in
                      PrgH but less extended than in YscD. Small-angle X-ray
                      scattering data show that also in solution this CdsD
                      construct adopts the same elongated shape. In both crystal
                      forms the CdsD molecules are packed in a parallel fashion,
                      using translational crystallographic symmetry. The most
                      extensive crystal contacts are preserved in both crystal
                      forms, suggesting a possible mode of assembly of the CdsD
                      periplasmic part into a 24-mer complex forming the outer
                      ring of the IM-ring of the T3SS.},
      cin          = {EMBL / EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-20120731 / I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (POF3-622) / BIOSTRUCT-X - Transnational
                      access and enhancement of integrated Biological Structure
                      determination at synchrotron X-ray radiation facilities
                      (283570)},
      pid          = {G:(DE-HGF)POF3-6G3 / G:(EU-Grant)283570},
      experiment   = {EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000374686900005},
      pubmed       = {pmid:26914207},
      doi          = {10.1002/pro.2906},
      url          = {https://bib-pubdb1.desy.de/record/321838},
}