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1HBZ

Catalase from Micrococcus lysodeikticu

Summary for 1HBZ
Entry DOI10.2210/pdb1hbz/pdb
DescriptorCATALASE, PROTOPORPHYRIN IX CONTAINING FE, SULFATE ION, ... (4 entities in total)
Functional Keywordsoxidoreductase, peroxidase, iron, heme hydrogen peroxide
Biological sourceMICROCOCCUS LYSODEIKTICUS
Total number of polymer chains1
Total formula weight57019.43
Authors
Murshudov, G.N.,Grebenko, A.I.,Barynin, V.V.,Braningen, J.,Wilson, K.S.,Dauter, Z.,Melik-Adamyan, W.R. (deposition date: 2001-04-24, release date: 2001-05-24, Last modification date: 2024-05-08)
Primary citationMurshudov, G.N.,Melik-Adamyan, W.R.,Grebenko, A.I.,Barynin, V.V.,Vagin, A.A.,Vainshtein, B.K.,Dauter, Z.,Wilson, K.S.
Three-Dimensional Structure of Catalase from Micrococcus Lysodeikticus at 1.5A Resolution
FEBS Lett., 312:127-, 1992
Cited by
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.
PubMed: 1426241
DOI: 10.1016/0014-5793(92)80919-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

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