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@ARTICLE{Wang:602310,
      author       = {Wang, Chu and Nehls, Christian and Baabe, Dirk and
                      Burghaus, Olaf and Hurwitz, Robert and Gutsmann, Thomas and
                      Bröring, Martin and Kolbe, Michael},
      title        = {{F}lagellin lysine methyltransferase {F}li{B} catalyzes a
                      [4{F}e-4{S}] mediated methyl transfer reaction},
      journal      = {PLoS pathogens},
      volume       = {17},
      number       = {11},
      issn         = {1553-7366},
      address      = {Lawrence, Kan.},
      publisher    = {PLoS},
      reportid     = {PUBDB-2024-00585},
      pages        = {e1010052 -},
      year         = {2021},
      abstract     = {The methyltransferase FliB posttranslationally modifies
                      surface-exposed ɛ-N-lysine residues of flagellin, the
                      protomer of the flagellar filament in Salmonella enterica
                      (S. enterica). Flagellin methylation, reported originally in
                      1959, was recently shown to enhance host cell adhesion and
                      invasion by increasing the flagellar hydrophobicity. The
                      role of FliB in this process, however, remained enigmatic.
                      In this study, we investigated the properties and mechanisms
                      of FliB from S. enterica in vivo and in vitro. We show that
                      FliB is an S-adenosylmethionine (SAM) dependent
                      methyltransferase, forming a membrane associated oligomer
                      that modifies flagellin in the bacterial cytosol. Using
                      X-band electron paramagnetic resonance (EPR) spectroscopy,
                      zero-field 57Fe Mössbauer spectroscopy, methylation assays
                      and chromatography coupled mass spectrometry (MS) analysis,
                      we further found that FliB contains an oxygen sensitive
                      [4Fe-4S] cluster that is essential for the methyl transfer
                      reaction and might mediate a radical mechanism. Our data
                      indicate that the [4Fe-4S] cluster is coordinated by a
                      cysteine rich motif in FliB that is highly conserved among
                      multiple genera of the Enterobacteriaceae family.},
      cin          = {CSSB-HZI-MK},
      ddc          = {610},
      cid          = {I:(DE-H253)CSSB-HZI-MK-20210520},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / FUTURE T3SS - Bacterial
                      effector secretion: Function and Architecture of the Type 3
                      Secretion System (311374)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(EU-Grant)311374},
      experiment   = {EXP:(DE-H253)P-P11-20150101 / EXP:(DE-H253)P-P12-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34788341},
      UT           = {WOS:000750695600014},
      doi          = {10.1371/journal.ppat.1010052},
      url          = {https://bib-pubdb1.desy.de/record/602310},
}