Abstract
The structure of the enzyme p-hydroxybenzoate hydroxylase (EC 1.14.13.2) in a complex with its substrate has been determined at a resolution of 2.5 Å. The molecular weight is 43,000 and the dimensions of one molecule are approximately 70 Å × 50 Å × 45 Å. The crystal structure contains dimers of these molecules. Approximately 16% of the residues occur in β-sheets and 26% in α-heliees. The molecule can be divided into three domains. The active site, near the isoalloxazine ring, is formed by side-chains of the three domains. The N-5 edge of the isoalloxazine ring points to p-hydroxybenzoate, which is bound in a deep cleft.
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