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Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution


Crystal structure of manganese superoxide dismutase from Bacillus stearothermophilus at 2.4 A resolution



Journal of Molecular Biology 199(4): 649-661



ISSN/ISBN: 0022-2836

PMID: 3351946

DOI: 10.1016/0022-2836(88)90308-7

The crystal structure of manganese superoxide dismutase (MnSOD) from Bacillus stearothermophilus has been solved at 2.4 .ANG. resolution by a combination of multiple isomorphous replacement and molecular replacement (1 .ANG. = 0.1 nm). The structure has been refined to a conventional R-factor for all 16,560 unique reflections at 2.4 .ANG. of 0.26, and the 2Fo.sbd.Fc density maps show features more consistent with the known amino acid sequence of MnSOD from B. stearothermophilus than with the starting model, the MnSOD from Thermus thermophilus. The molecule is a dimer of identical subunits, each with 203 amino acid residues. The polypeptide chain of the monomer is organized into two domains, one of which has an "all-.alpha." structure and the other an ".alpha./.beta." structure, with the manganese ion bound between them. The ion is co-ordinated by three histidine residues, 26, 81 and 167, and one aspartic acid residue, 173, in a tetrahedral arrangement strongly distorted towards trigonal pyrmidal. We anticipate that Tyr34, whose hydroxyl group is only 5 .ANG. from the metal, is involved in the catalytic reaction. The active site is particularly rich in aromatic amino acid residues. As in the Cu/ZnSOD there are indications that MnSOD provides electrostatic guidance to the substrate entering the active site.

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Accession: 005072254

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