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Structures of two highly homologous bacterial L-asparaginases: a case of enantiomorphic space groups

  1. Author:
    Jaskolski, M.
    Kozak, M.
    Lubkowski, J.
    Palm, G.
    Wlodawer, A.
  2. Author Address

    Adam Mickiewicz Univ, Fac Chem, Dept Crystallog, Grunwaldzka 6, Poznan, Poland. Adam Mickiewicz Univ, Fac Chem, Dept Crystallog, Poznan, Poland. Polish Acad Sci, Inst Bioorgan Chem, Ctr Biocrystallog Res, Poznan, Poland. Adam Mickiewicz Univ, Fac Phys, Dept Macromol Phys, Poznan, Poland. NCI, Macromol Crystallog Lab, Program Struct Biol, Frederick Canc Res & Dev Ctr, Frederick, MD 21702 USA. Wlodawer A Adam Mickiewicz Univ, Fac Chem, Dept Crystallog, Grunwaldzka 6, Poznan, Poland.
    1. Year: 2001
  1. Journal: Acta Crystallographica Section D-Biological Crystallography
    1. 57
    2. Pt. 3
    3. Pages: 369-377
  2. Type of Article: Article
  1. Abstract:

    Quasi-enantiomorphic crystals of the Y25F mutant of Escherichia coli L-asparaginase and of the native Erwinia chrysanthemi L- asparaginase were obtained in the hexagonal space groups P6(5)22 and P6(1)22, respectively. The structures of these highly homologous enzymes were solved by molecular replacement and were refined with data extending to 2.2-2.5 Angstrom. These structures were compared with each other, as well as with other L-asparaginase structures previously observed with different crystal packing. It is concluded that the observed phenomenon, which is rare, was most likely to have arisen by chance.

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