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@ARTICLE{Bunduc:457180,
      author       = {Bunduc, Catalin and Fahrenkamp, Dirk and Wald, Jiri and
                      Ummels, Roy and bitter, wilbert and Houben, Edith and
                      Marlovits, Thomas},
      title        = {{S}tructure and dynamics of a mycobacterial type {VII}
                      secretion system},
      journal      = {Nature},
      volume       = {593},
      number       = {7859},
      issn         = {0028-0836},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {PUBDB-2021-01909},
      pages        = {445 - 448},
      year         = {2021},
      note         = {Cryo EM},
      abstract     = {Mycobacterium tuberculosis is the cause of one of the most
                      important infectious diseases in humans, which leads to 1.4
                      million deaths every year1. Specialized protein transport
                      systems—known as type VII secretion systems (T7SSs)—are
                      central to the virulence of this pathogen, and are also
                      crucial for nutrient and metabolite transport across the
                      mycobacterial cell envelope2,3. Here we present the
                      structure of an intact T7SS inner-membrane complex of M.
                      tuberculosis. We show how the 2.32-MDa ESX-5 assembly, which
                      contains 165 transmembrane helices, is restructured and
                      stabilized as a trimer of dimers by the MycP$_5$ protease. A
                      trimer of MycP$_5$ caps a central periplasmic dome-like
                      chamber that is formed by three EccB$_5$ dimers, with the
                      proteolytic sites of MycP$_5$ facing towards the cavity.
                      This chamber suggests a central secretion and processing
                      conduit. Complexes without MycP$_5$ show disruption of the
                      EccB5 periplasmic assembly and increased flexibility, which
                      highlights the importance of MycP$_5$ for complex integrity.
                      Beneath the EccB$_5$–MycP$_5$ chamber, dimers of the EccC5
                      ATPase assemble into three bundles of four transmembrane
                      helices each, which together seal the potential central
                      secretion channel. Individual cytoplasmic EccC5 domains
                      adopt two distinctive conformations that probably reflect
                      different secretion states. Our work suggests a previously
                      undescribed mechanism of protein transport and provides a
                      structural scaffold to aid in the development of drugs
                      against this major human pathogen.},
      cin          = {FS-PS / CSSB-UKE},
      ddc          = {500},
      cid          = {I:(DE-H253)FS-PS-20131107 / I:(DE-H253)CSSB-UKE-20141216},
      pnm          = {633 - Life Sciences – Building Blocks of Life: Structure
                      and Function (POF4-633) / CryoMyco - Atomic dissection of
                      type VII secretion systems from pathogenic mycobacteria
                      (101030373)},
      pid          = {G:(DE-HGF)POF4-633 / G:(EU-Grant)101030373},
      experiment   = {EXP:(DE-MLZ)NOSPEC-20140101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33981042},
      UT           = {WOS:000650174400004},
      doi          = {10.1038/s41586-021-03517-z},
      url          = {https://bib-pubdb1.desy.de/record/457180},
}