Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5 A resolution.
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.
Murshudov
G N
GN
Institute of Crystallography, Russian Academy of Sciences, Moscow.
Melik-Adamyan
W R
WR
Grebenko
A I
AI
Barynin
V V
VV
Vagin
A A
AA
Vainshtein
B K
BK
Dauter
Z
Z
Wilson
K S
KS
D000595:Amino Acid Sequence; D005075:Biological Evolution; D002374:Catalase / Q000737:chemistry* / Q000378:metabolism; D008837:Micrococcus / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D002374:Catalase