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@ARTICLE{Prakash:642752,
      author       = {Prakash, Ohm and Führing, Jana and Baruch, Petra and
                      Fedorov, Roman and Routier, Françoise H.},
      title        = {{T}he post-reactive structures of {L}eishmania major
                      {UDP}-sugar pyrophosphorylase provide insights into the
                      product release mechanism},
      journal      = {Microbiology spectrum},
      volume       = {13},
      number       = {11},
      issn         = {2165-0497},
      address      = {Birmingham, Ala.},
      publisher    = {ASM},
      reportid     = {PUBDB-2025-05601},
      pages        = {e00911-25},
      year         = {2025},
      abstract     = {Biosynthesis of the nucleotide sugars UDP-glucose (UDP-Glc)
                      and UDP-galactose (UDP-Gal) is intimately connected and
                      essential for the viability of trypanosomatid parasites. In
                      the genus Leishmania, it is controlled by the UDP-glucose
                      pyrophosphorylase (UGP) and UDP-sugar pyrophosphorylase
                      (USP). In contrast to UGP, USP has a broad substrate
                      specificity and may generate several UDP-sugars in vitro,
                      including UDP-Glc and UDP-Gal. This enzyme, present in
                      protozoan parasites (including Leishmania species and
                      Trypanosoma cruzi) and in plants, most likely plays a role
                      in salvaging monosaccharides. In order to gain a detailed
                      mechanistic understanding of USPs, we determined
                      high-resolution X-ray structures of Leishmania major USP
                      (LmUSP) in post-reactive states. Several positions of the
                      byproduct pyrophosphate (PPi) were identified and revealed a
                      product release channel in the forward reaction, as well as
                      the geometries of post-reactive Michaelis product complexes.
                      The conformational changes of functional loops (hinge
                      loop-1, hinge loop-2, and the nucleotide-binding loop)
                      showed dynamic effects accompanying the product release
                      process. Structural information about the post-reactive
                      states of LmUSP also includes the metastable binding
                      position of a magnesium (Mg2+) ion in the active site. The
                      proposed product release mechanism was substantiated by
                      molecular dynamics simulations and can serve as a model for
                      other UDP-sugar pyrophosphorylases.},
      cin          = {EMBL-User},
      ddc          = {570},
      cid          = {I:(DE-H253)EMBL-User-20120814},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3) / DFG project
                      G:(GEPRIS)390874280 - EXC 2155: RESIST - Resolving Infection
                      Susceptibility (390874280)},
      pid          = {G:(DE-HGF)POF4-6G3 / G:(GEPRIS)390874280},
      experiment   = {EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      doi          = {10.1128/spectrum.00911-25},
      url          = {https://bib-pubdb1.desy.de/record/642752},
}