% 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{Williams:166793,
      author       = {Williams, Chris and van den Berg, Marlene and Stanley, Will
                      A. and Wilmanns, Matthias and Distel, Ben},
      title        = {{A} disulphide bond in the {E}2 enzyme {P}ex4p modulates
                      ubiquitin-conjugating activity},
      journal      = {Scientific reports},
      volume       = {3},
      issn         = {2045-2322},
      address      = {London},
      publisher    = {Nature Publishing Group},
      reportid     = {DESY-2014-01627},
      pages        = {2212},
      year         = {2013},
      abstract     = {The ubiquitin-conjugating enzyme Pex4p together with its
                      binding partner, the peroxisomal membrane protein Pex22p,
                      co-ordinates cysteine-dependent ubiquitination of the
                      cycling receptor protein Pex5p. Unusually for an
                      ubiquitin-conjugating enzyme, Saccharomyces cerevisiae Pex4p
                      can form a disulphide bond between the cysteine residues at
                      positions 105 and 146. We found that mutating the disulphide
                      forming cysteine residues in Pex4p to serines does not
                      disturb the secondary structure of the protein but does
                      reduce the in vitro activity of Pex4p. From the crystal
                      structure of Pex4p C105S, C146S in complex with the soluble
                      domain of Pex22p, we observe a narrowing of the active site
                      cleft, caused by loss of the disulphide bond. This
                      modification of the active site microenvironment is likely
                      to restrict access of ubiquitin to the active site cysteine,
                      modulating Pex4p activity. Finally, based on sequence and
                      structural alignments, we have identified other
                      ubiquitin-conjugating enzymes that may contain disulphide
                      bonds.},
      cin          = {EMBL},
      ddc          = {000},
      cid          = {I:(DE-H253)EMBL-20120731},
      pnm          = {DORIS Beamline K1.3 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-K1.3-20130405},
      experiment   = {EXP:(DE-H253)D-K1.3-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000322433200001},
      pubmed       = {pmid:23896733},
      doi          = {10.1038/srep02212},
      url          = {https://bib-pubdb1.desy.de/record/166793},
}