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@ARTICLE{Groves:399602,
      author       = {Groves, Matthew R. and Schroer, Carsten F. E. and
                      Middleton, Adam J. and Lunev, Sergey and Danda, Natasha and
                      Ali, Ameena M. and Marrink, Siewert J. and Williams, Chris},
      title        = {{S}tructural insights into {K}48-linked ubiquitin chain
                      formation by the {P}ex4p-{P}ex22p complex},
      journal      = {Biochemical and biophysical research communications},
      volume       = {496},
      number       = {2},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PUBDB-2018-00778},
      pages        = {562 - 567},
      year         = {2017},
      abstract     = {Pex4p is a peroxisomal E2 involved in ubiquitinating the
                      conserved cysteine residue of the cycling receptor protein
                      Pex5p. Previously, we demonstrated that Pex4p from the yeast
                      Saccharomyces cerevisiae binds directly to the peroxisomal
                      membrane protein Pex22p and that this interaction is vital
                      for receptor ubiquitination. In addition, Pex22p binding
                      allows Pex4p to specifically produce lysine 48 linked
                      ubiquitin chains in vitro through an unknown mechanism. This
                      activity is likely to play a role in targeting peroxisomal
                      proteins for proteasomal degradation.Here we present the
                      crystal structures of Pex4p alone and in complex with Pex22p
                      from the yeast Hansenula polymorpha. Comparison of the two
                      structures demonstrates significant differences to the
                      active site of Pex4p upon Pex22p binding while molecular
                      dynamics simulations suggest that Pex22p binding facilitates
                      active site remodelling of Pex4p through an allosteric
                      mechanism. Taken together, our data provide insights into
                      how Pex22p binding allows Pex4p to build K48-linked Ub
                      chains.},
      cin          = {DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (POF3-622)},
      pid          = {G:(DE-HGF)POF3-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29288668},
      UT           = {WOS:000424313500048},
      doi          = {10.1016/j.bbrc.2017.12.150},
      url          = {https://bib-pubdb1.desy.de/record/399602},
}