Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 Å resolution

• Published in: FEBS letters Vol. 312; no. 2; pp. 127 - 131
• Main Authors: Murshudov, G.N., Melik-Adamyan, W.R., Grebenko, A.I., Barynin, V.V., Vagin, A.A., Vainshtein, B.K., Dauter, Z., Wilson, K.S.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 09.11.1992; Elsevier
• Subjects: Amino Acid Sequence; Biological and medical sciences; Biological Evolution; Catalase; Catalase - chemistry; Catalase - metabolism; Crystalline structure; Fundamental and applied biological sciences. Psychology; Micrococcus - enzymology; Micrococcus lysodeikticus; Models, Molecular; Molecular biophysics; Molecular Sequence Data; Protein Conformation; Sequence Homology, Amino Acid; Structure in molecular biology; X-Ray Diffraction; X-Ray structure; Catalase; X-Ray structure; Micrococcus lysodeikticus; Enzyme; Computerized processing; Refinement; Bacteria; Micrococcales; Micrococcaceae; X ray diffraction; Micrococcus luteus; Spatial structure; Aminoacid sequence; Crystalline structure
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(92)80919-8

The three-dimensional crystal structure of catalase from Micrococcus lysodeikticus has been solved by multiple isomorphous replacement and refined at 1.5 Å resolution. The subunit of the tetrameric molecule of 222 symmetry consists of a single polypeptide chain of about 500 amino acid residues and one haem group. The crystals belong to space group P4 22 12 with unit cell parameters a = b = 106,7 Å, c = 106,3 Å, and there is one subunit of the tetramer. per asymmetric unit. The amino acid sequence has been tentatively determined by computer graphics model building and comparison with the known three-dimensional structure of beef liver catalase and sequences of several other catalases. The atomic model has been refined by Hendrickson and Konnert's least-squares minimisation against 94,315 reflections between 8 Å and 1.5 Å. The final model consists or 3,977 non-hydrogen atoms of the protein and haem group, 426 water molecules and ones sulphate ion. The secondary and tertiary sructures of the bacterial catalase have been analyzed and a comparison with the structure of beef liver catalase has been made.