% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Zhang:207430,
      author       = {Zhang, Gongyi and Mertens, Haydyn and Garefalaki, Vasiliki
                      and Jeffries, Cy and Thompson, Andrew and Lemke, Edward A.
                      and Svergun, Dmitri and Mayer, Melinda J. and Narbad, Arjan
                      and Meijers, Rob and Zhang, Gongyi},
      title        = {{T}he {CD}27{L} and {CTP}1{L} {E}ndolysins {T}argeting
                      {C}lostridia {C}ontain a {B}uilt-in {T}rigger and {R}elease
                      {F}actor},
      journal      = {PLoS pathogens},
      volume       = {10},
      number       = {7},
      issn         = {1553-7374},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2015-01340},
      pages        = {e1004228 -},
      year         = {2014},
      note         = {OA},
      abstract     = {The bacteriophage ΦCD27 is capable of lysing Clostridium
                      difficile, a pathogenic bacterium that is a major cause for
                      nosocomial infection. A recombinant CD27L endolysin lyses C.
                      difficile in vitro, and represents a promising alternative
                      as a bactericide. To better understand the lysis mechanism,
                      we have determined the crystal structure of an
                      autoproteolytic fragment of the CD27L endolysin. The
                      structure covers the C-terminal domain of the endolysin, and
                      represents a novel fold that is identified in a number of
                      lysins that target Clostridia bacteria. The structure
                      indicates endolysin cleavage occurs at the stem of the
                      linker connecting the catalytic domain with the C-terminal
                      domain. We also solved the crystal structure of the
                      C-terminal domain of a slow cleaving mutant of the CTP1L
                      endolysin that targets C. tyrobutyricum. Two distinct
                      dimerization modes are observed in the crystal structures
                      for both endolysins, despite a sequence identity of only
                      $22\%$ between the domains. The dimers are validated to be
                      present for the full length protein in solution by right
                      angle light scattering, small angle X-ray scattering and
                      cross-linking experiments using the cross-linking amino acid
                      p-benzoyl-L-phenylalanine (pBpa). Mutagenesis on residues
                      contributing to the dimer interfaces indicates that there is
                      a link between the dimerization modes and the autocleavage
                      mechanism. We show that for the CTP1L endolysin, there is a
                      reduction in lysis efficiency that is proportional to the
                      cleavage efficiency. We propose a model for endolysin
                      triggering, where the extended dimer presents the inactive
                      state, and a switch to the side-by-side dimer triggers the
                      cleavage of the C-terminal domain. This leads to the release
                      of the catalytic portion of the endolysin, enabling the
                      efficient digestion of the bacterial cell wall.},
      cin          = {EMBL},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline K1.2 (POF2-54G13) / PETRA Beamline P14
                      (POF2-54G14)},
      pid          = {G:(DE-H253)POF2-K1.2-20130405 /
                      G:(DE-H253)POF2-P14-20130405},
      experiment   = {EXP:(DE-H253)D-K1.2-20150101 / EXP:(DE-H253)P-P14-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000340551000023},
      pubmed       = {pmid:25058163},
      doi          = {10.1371/journal.ppat.1004228},
      url          = {https://bib-pubdb1.desy.de/record/207430},
}