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@ARTICLE{Gierse:546331,
      author       = {Gierse, Robin M. and Reddem, Eswar R. and Alhayek, Alaa and
                      Baitinger, Dominik and Hamid, Zhoor and Jakobi, Harald and
                      Laber, Bernd and Lange, Gudrun and Hirsch, Anna K. H. and
                      Groves, Matthew},
      title        = {{I}dentification of a 1-deoxy-{D}-xylulose-5-phosphate
                      synthase ({DXS}) mutant with improved crystallographic
                      properties},
      journal      = {Biochemical and biophysical research communications},
      volume       = {539},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {PUBDB-2023-00645},
      pages        = {42 - 47},
      year         = {2021},
      abstract     = {In this report, we describe a truncated Deinococcus
                      radiodurans 1-deoxy-D-xylulose-5-phosphate synthase (DXS)
                      protein that retains enzymatic activity, while slowing
                      protein degradation and showing improved crystallization
                      properties. With modern drug-design approaches relying
                      heavily on the elucidation of atomic interactions of
                      potential new drugs with their targets, the need for
                      co-crystal structures with the compounds of interest is
                      high. DXS itself is a promising drug target, as it catalyzes
                      the first reaction in the 2-C-methyl-D-erythritol
                      4-phosphate (MEP)-pathway for the biosynthesis of the
                      universal precursors of terpenes, which are essential
                      secondary metabolites. In contrast to many bacteria and
                      pathogens, which employ the MEP pathway, mammals use the
                      distinct mevalonate-pathway for the biosynthesis of these
                      precursors, which makes all enzymes of the MEP-pathway
                      potential new targets for the development of
                      anti-infectives. However, crystallization of DXS has proven
                      to be challenging: while the first X-ray structures from
                      Escherichia coli and D. radiodurans were solved in 2004,
                      since then only two additions have been made in 2019 that
                      were obtained under anoxic conditions. The presented site of
                      truncation can potentially also be transferred to other
                      homologues, opening up the possibility for the determination
                      of crystal structures from pathogenic species, which until
                      now could not be crystallized. This manuscript also provides
                      a further example that truncation of a variable region of a
                      protein can lead to improved structural data.},
      cin          = {DOOR ; HAS-User},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {6G3 - PETRA III (DESY) (POF4-6G3)},
      pid          = {G:(DE-HGF)POF4-6G3},
      experiment   = {EXP:(DE-H253)P-P11-20150101 / EXP:(DE-H253)P-P13-20150101},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:33421767},
      UT           = {WOS:000613422000007},
      doi          = {10.1016/j.bbrc.2020.12.069},
      url          = {https://bib-pubdb1.desy.de/record/546331},
}