Three-dimensional structure of catalase from Penicillium vitale at 2.0 A resolution

J Mol Biol. 1986 Mar 5;188(1):49-61. doi: 10.1016/0022-2836(86)90479-1.


The three-dimensional structure analysis of crystalline fungal catalase from Penicillium vitale has been extended to 2.0 A resolution. The crystals belong to space group P3(1)21, with the unit cell parameters of a = b = 144.4 A and c = 133.8 A. The asymmetric unit contains half a tetrameric molecule of 222 symmetry. Each subunit is a single polypeptide chain of approximately 670 amino acid residues and binds one heme group. The amino acid sequence has been tentatively determined by computer graphics model building (using the FRODO system) and comparison with the known sequence of beef liver catalase. The atomic model has been refined by the Hendrickson & Konnert (1981) restrained least-squares program against 68,000 reflections between 5 A and 2 A resolution. The final R-factor is 0.31 after 24 refinement cycles. The secondary and tertiary structure of the catalase has been analyzed.

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Catalase*
  • Crystallography
  • Heme
  • Hydrogen Bonding
  • Macromolecular Substances
  • Models, Molecular
  • Penicillium / enzymology*
  • Protein Conformation


  • Amino Acids
  • Macromolecular Substances
  • Heme
  • Catalase