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@ARTICLE{Klimenko:642754,
      author       = {Klimenko, Victoria and Reiners, Jens and Applegate,
                      Violetta and Reimann, Katharina and Popowicz, Grzegorz and
                      Port, Astrid and Papadopoulos, Athanasios and Smits, Sander
                      and Nowack, Eva C M},
      title        = {{T}he {P}aulinella chromatophore transit peptide part2
                      adopts a structural fold similar to the
                      γ-glutamyl-cyclotransferase fold},
      journal      = {Plant physiology},
      volume       = {199},
      number       = {2},
      issn         = {0032-0889},
      address      = {Oxford},
      publisher    = {Oxford University Press},
      reportid     = {PUBDB-2025-05603},
      pages        = {kiaf504},
      year         = {2025},
      abstract     = {The chromatophores of the cercozoan amoeba Paulinella are
                      photosynthetic organelles that evolved from a cyanobacterial
                      endosymbiont. Many nucleus-encoded chromatophore-targeted
                      proteins carry unusual N-terminal targeting signals termed
                      crTPs, which are bipartite. crTPpart1 likely mediates
                      trafficking through the secretory pathway and is cleaved off
                      during import, but crTPpart2 remains attached to its cargo
                      protein and its function is unknown. To unravel the
                      functional role of crTPpart2, here we elucidated the
                      structures of crTPpart2 from two different
                      chromatophore-targeted proteins by X-ray crystallography at
                      ∼2.3 Å resolution. Interestingly, the crTPpart2 of both
                      proteins adopts a structural fold. Both structures share a
                      conserved structured core and a flexible N-terminal arm. The
                      structured core resembles proteins of the γ-glutamyl
                      cyclotransferase superfamily within which crTPpart2
                      structures form a protein (sub)-family. The proposed
                      catalytic center typical for proteins with cyclotransferase
                      activity is not conserved in crTPpart2. A Cys pair that is
                      conserved in crTPpart2 of many chromatophore-targeted
                      proteins has been captured as a disulfide bridge. Together,
                      our data suggest that chromatophore-targeted proteins are
                      imported in their folded state and that the fold adopted by
                      crTPpart2 plays a functional role during import. The
                      characterization of its structure and flexibility provides
                      important steps toward elucidating this protein
                      translocation mechanism.},
      cin          = {EMBL-User},
      ddc          = {580},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P12-20150101 / EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1093/plphys/kiaf504},
      url          = {https://bib-pubdb1.desy.de/record/642754},
}