Download MendeleyThree-Dimensional Structure of Catalase from Micrococcus Lysodeikticus at 1.5A Resolution
Murshudov, G.N., Melik-Adamyan, W.R., Grebenko, A.I., Barynin, V.V., Vagin, A.A., Vainshtein, B.K., Dauter, Z., Wilson, K.S.(1992) FEBS Lett 312: 127
- PubMed: 1426241
- DOI: https://doi.org/10.1016/0014-5793(92)80919-8
- Primary Citation of Related Structures:
1HBZ - PubMed Abstract:
The three-dimensional crystal structure of catalase from Micrococcus lysodeikticus has been solved by multiple isomorphous replacement and refined at 1.5 A 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(2)2(1)2 with unit cell parameters a = b = 106.7 A, c = 106.3 A, 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 A and 1.5 A. The final model consists of 3,977 non-hydrogen atoms of the protein and haem group, 426 water molecules and one sulphate ion. The secondary and tertiary structures of the bacterial catalase have been analyzed and a comparison with the structure of beef liver catalase has been made.
Organizational Affiliation:
Institute of Crystallography, Russian Academy of Sciences, Moscow.
