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@ARTICLE{Botte:825205,
      author       = {Botte, Mathieu and Zaccai, Nathan R. and Nijeholt, Jelger
                      Lycklama à. and Martin, Remy and Knoops, Kèvin and Papai,
                      Gabor and Zou, Juan and Deniaud, Aurélien and Karuppasamy,
                      Manikandan and Jiang, Qiyang and Roy, Abhishek Singha and
                      Schulten, Klaus and Schultz, Patrick and Rappsilber, Juri
                      and Zaccai, Giuseppe and Berger, Imre and Collinson, Ian and
                      Schaffitzel, Christiane},
      title        = {{A} central cavity within the holo-translocon suggests a
                      mechanism for membrane protein insertion},
      journal      = {Scientific reports},
      volume       = {6},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {FZJ-2016-07676},
      pages        = {38399 -},
      year         = {2016},
      abstract     = {The conserved SecYEG protein-conducting channel and the
                      accessory proteins SecDF-YajC and YidC constitute the
                      bacterial holo-translocon (HTL), capable of
                      protein-secretion and membrane-protein insertion. By
                      employing an integrative approach combining small-angle
                      neutron scattering (SANS), low-resolution electron
                      microscopy and biophysical analyses we determined the
                      arrangement of the proteins and lipids within the
                      super-complex. The results guided the placement of X-ray
                      structures of individual HTL components and allowed the
                      proposal of a model of the functional translocon. Their
                      arrangement around a central lipid-containing pool conveys
                      an unexpected, but compelling mechanism for membrane-protein
                      insertion. The periplasmic domains of YidC and SecD are
                      poised at the protein-channel exit-site of SecY, presumably
                      to aid the emergence of translocating polypeptides. The SecY
                      lateral gate for membrane-insertion is adjacent to the
                      membrane ‘insertase’ YidC. Absolute-scale SANS employing
                      a novel contrast-match-point analysis revealed a dynamic
                      complex adopting open and compact configurations around an
                      adaptable central lipid-filled chamber, wherein polytopic
                      membrane-proteins could fold, sheltered from aggregation and
                      proteolysis.},
      cin          = {JCNS (München) ; Jülich Centre for Neutron Science JCNS
                      (München) ; JCNS-FRM-II},
      ddc          = {000},
      cid          = {I:(DE-Juel1)JCNS-FRM-II-20110218},
      pnm          = {6G15 - FRM II / MLZ (POF3-6G15) / 6G4 - Jülich Centre for
                      Neutron Research (JCNS) (POF3-623)},
      pid          = {G:(DE-HGF)POF3-6G15 / G:(DE-HGF)POF3-6G4},
      experiment   = {EXP:(DE-MLZ)KWS2-20140101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000389740800001},
      pubmed       = {pmid:27924919},
      doi          = {10.1038/srep38399},
      url          = {https://juser.fz-juelich.de/record/825205},
}