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

FEBS Letters

Vagin, A.A.¹  Dauter, Z.²  Murshudov, G.N.¹  Barynin, V.V.¹  Vainshtein, B.K.¹  Wilson, K.S.²  Grebenko, A.I.¹  Melik-Adamyan, W.R.¹ 

[1] Institute of Crystallography, Russian Academy of Sciences, Leninsky pr. 59, Moscow 117333, Russia;European Molecular Biology Laboratory (EMBL). c/o DESY, Notkestrasse 85, Hamburg 52, Germany

关键词: Catalase;    X-Ray structure;    Micrococcus lysodeikticus;   

DOI  :  10.1016/0014-5793(92)80919-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 P4₂2₁2 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.

【 授权许可】

Unknown