Comparison of beef liver and Penicillium vitale catalases

William Melik-Adamyan, R. ; Vladimir Barynin, V. ; Alexey Vagin, A. ; Vsevolod Borisov, V. ; Boris Vainshtein, K. ; Fita, Ignacio ; Mathur Murthy, R. N. ; Rossmann, G. Michael (1986) Comparison of beef liver and Penicillium vitale catalases Journal of Molecular Biology, 188 (1). pp. 63-72. ISSN 0022-2836

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The structures of Penicillium vitale and beef liver catalase have been determined to atomic resolution. Both catalases are tetrameric proteins with deeply buried heme groups. The amino acid sequence of beef liver catalase is known and contains (at least) 506 amino acid residues. Although the sequence of P. vitale catalase has not yet been determined chemically, 670 residues have been built into the 2 Å resolution electron density map and have been given tentative assignments. A large portion of each catalase molecule (91% of residues in beef liver catalase and 68% of residues in P. vitale catalase) shows structural homology. The root-mean-square deviation between 458 equivalenced Cα atoms is 1.17 Å . The dissimilar parts include a small fragment of the N-terminal arm and an additional "flavodoxin-like" domain at the carboxy end of the polypeptide chain of P. vitale catalase. In contrast, beef liver catalase contains one bound NADP molecule per subunit in a position equivalent to the chain region, leading to the flavodoxin-like domain, of P. vitale catalase. The position and orientation of the buried heme group in the two catalases, relative to the mutually perpendicular molecular dyad axes, are identical within experimental error. A mostly hydrophobic channel leads to the buried heme group. The surface opening to the channel differs due to the different disposition of the amino-terminal arm and the presence of the additional flavodoxin-like domain in P. vitale catalase. Possible functional implications of these comparisons are discussed.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:74837
Deposited On:19 Dec 2011 12:13
Last Modified:19 Dec 2011 12:13

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