Journal of Molecular Biology
Volume 152, Issue 2, 25 October 1981, Pages 465-486, IN1, 487-499
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Structure of beef liver catalase

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Abstract

The three-dimensional structure of beef liver catalase has been determined to 2.5 å resolution by a combination of isomorphous and molecular replacement techniques. Heavy-atom positions were found using vector search and difference Fourier methods. The tetrameric catalase molecule has 222 symmetry with one of its dyads coincident with a crystallographic 2-fold axis. The known polypeptide sequence has been unambiguously fitted to the electron density map. The heme is well buried in a hydrophobic pocket, 20 Å below the surface of the molecule, and accessible through a hydrophobic channel. Residues that line the heme pocket belong to two different subunits. Tyr357 is the proximal heme ligand and the catalytically important residues on the distal side are residues His74 and Asnl47. The tertiary structure consists of four domains: an extended non-globular amino-terminal arm, which stabilizes the quaternary structure; an anti-parallel, eight-stranded β-barrel providing the residues on the distal side of the heme; a rather random “wrapping domain” around the subunit exterior including the proximal heme ligand; and a final λ-helical structure resembling the E, F, G and H helices of the globins.

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    The work was supported by the National Institutes of Health (grant no. GM10704) and the National Science Foundation (grant no. PCM78-16584). One author (T.J.R.) was supported by a National Institutes of Health Cellular and Molecular Biology Grant and another (A.S.) by a National Institutes of Health Postdoctoral Fellowship (no. 1 F32 GM06364) during part of this work.

    Present address: Uniformed Services, University of the Health Sciences, Bethesda, Md. U.S.A.

    §

    Present address: Institute for Protein Research, Osaka University, 5311, Yamada-kami, Suita, Osaka, Japan.

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