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@ARTICLE{Piasecka:417860,
      author       = {Piasecka, Anna and Czapinska, Honorata and Vielberg,
                      Marie-Theres and Szczepanowski, Roman H. and Kiefersauer,
                      Reiner and Reed, Simon and Groll, Michael and Bochtler,
                      Matthias},
      title        = {{T}he {Y}. bercovieri {A}nbu crystal structure sheds light
                      on the evolution of highly (pseudo)symmetric multimers},
      journal      = {Journal of molecular biology},
      volume       = {430},
      number       = {5},
      issn         = {0022-2836},
      address      = {Amsterdam [u.a.]},
      publisher    = {Elsevier},
      reportid     = {PUBDB-2019-00036},
      pages        = {611 - 627},
      year         = {2018},
      abstract     = {Ancestral β-subunit (Anbu) is homologous to HslV and 20S
                      proteasomes. Based on its phylogenetic distribution and
                      sequence clustering, Anbu has been proposed as the
                      “ancestral” form of proteasomes. Here, we report
                      biochemical data, small-angle X-ray scattering results,
                      negative-stain electron microscopy micrographs and a crystal
                      structure of the Anbu particle from Yersinia bercovieri
                      (YbAnbu). All data are consistent with YbAnbu forming
                      defined 12–14 subunit multimers that differ in shape from
                      both HslV and 20S proteasomes. The crystal structure reveals
                      that YbAnbu subunits form tight dimers, held together in
                      part by the Anbu specific C-terminal helices. These dimers
                      (“protomers”) further assemble into a low-rise
                      left-handed staircase. The lock-washer shape of YbAnbu is
                      consistent with the presence of defined multimers, X-ray
                      diffraction data in solution and negative-stain electron
                      microscopy images. The presented structure suggests a
                      possible evolutionary pathway from helical filaments to
                      highly symmetric or pseudosymmetric multimer structures.
                      YbAnbu subunits have the Ntn-hydrolase fold, a putative S1
                      pocket and conserved candidate catalytic residues Thr1,
                      Asp17 and Lys32(33). Nevertheless, we did not detect any
                      YbAnbu peptidase or amidase activity. However, we could
                      document orthophosphate production from ATP catalyzed by the
                      ATP-grasp protein encoded in the Y. bercovieri Anbu operon.},
      cin          = {EMBL-User},
      ddc          = {610},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {899 - ohne Topic (POF3-899)},
      pid          = {G:(DE-HGF)POF3-899},
      experiment   = {EXP:(DE-H253)D-D1.2-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29258816},
      UT           = {WOS:000429398200006},
      doi          = {10.1016/j.jmb.2017.11.016},
      url          = {https://bib-pubdb1.desy.de/record/417860},
}