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@ARTICLE{Battula:166130,
      author       = {Battula, Pradeep and Dubnovitsky, Anatoly P. and
                      PAPAGEORGIOU, ANASTASSIOS},
      title        = {{S}tructural basis of {L} -phosphoserine binding to
                      {B}acillus alcalophilus phosphoserine aminotransferase},
      journal      = {Acta crystallographica / D},
      volume       = {69},
      number       = {5},
      issn         = {1399-0047},
      address      = {Copenhagen},
      publisher    = {Munksgaard},
      reportid     = {DESY-2014-01061},
      pages        = {804 - 811},
      year         = {2013},
      note         = {(c) International Union of Crystallography; Post referee
                      fulltext in progress},
      abstract     = {Phosphoserine aminotransferase is a vitamin B6-dependent
                      enzyme that catalyzes the reversible conversion of
                      3-­phosphohydroxypyruvate to L-phosphoserine using
                      glutamate as an amine donor. In an effort to gain insight
                      into the substrate-recognition mechanism of the enzyme,
                      crystal structures of Bacillus alcalophilus phosphoserine
                      aminotransferase in the presence or absence of
                      L-phosphoserine were determined to resolutions of 1.5 and
                      1.6 Å, respectively. Local conformational changes induced
                      upon substrate binding were identified. However, in contrast
                      to other aminotransferases, no domain or subunit movements
                      were observed. Two Arg residues (Arg42 and Arg328) and two
                      His residues (His41 and His327) were found to form a tight
                      binding site for the phosphate group of L-­phosphoserine.
                      Comparison with Escherichia coli phosphoserine
                      aminotransferase in complex with the substrate analogue
                      [alpha]-­methylglutamate revealed more extensive structural
                      changes in the case of L-phosphoserine binding. Based on the
                      structural analysis, the flexibility of Arg328 is proposed
                      to be critical for substrate recognition.},
      cin          = {DOOR},
      ddc          = {570},
      cid          = {I:(DE-H253)HAS-User-20120731},
      pnm          = {DORIS Beamline X1 (POF2-54G13)},
      pid          = {G:(DE-H253)POF2-X1-20130405},
      experiment   = {EXP:(DE-H253)D-X1-20150101},
      typ          = {PUB:(DE-HGF)16},
      UT           = {WOS:000318240200014},
      pubmed       = {pmid:23633589},
      doi          = {10.1107/S0907444913002096},
      url          = {https://bib-pubdb1.desy.de/record/166130},
}