1e5r

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Revision as of 19:40, 24 November 2007

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spinqualitylabelsall models 1e5r, resolution 2.3Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

PROLINE 3-HYDROXYLASE (TYPE II)-APO FORM

Overview

Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative, reactions in a range of metabolic processes including the hydroxylation of, proline and lysine residues during the post-translational modification of, collagen. 2-OG oxygenases commonly require ascorbate for full activity. In, the vitamin C deficient disease, scurvy, reduced activity of 2-OG, oxygenases results in impaired formation of collagen. Here we report the, crystal structure of bacterial proline 3-hydroxylase from Streptomyces, sp., an enzyme which hydroxylates proline at position 3, the first of a, 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. Structures, were obtained for the enzyme in the absence of iron (to 2.3A resolution, R=20.2%, Rfree=25.3%) and that complexed to iron (II) (to 2.4A resolution, R=19.8%, Rfree=22.6%). The structure contains conserved motifs present in, other 2-OG oxygenases including a 'jelly roll' beta strand core and, residues binding iron and 2-oxoglutarate, consistent with divergent, evolution within the extended family. The structure differs significantly, from many other 2-OG oxygenases in possessing a discrete C-terminal, helical domain. Analysis of the structure suggests a model for proline, binding and a mechanism for uncoupling of proline and 2-OG turnover.

About this Structure

1E5R is a Single protein structure of sequence from Streptomyces sp.. Full crystallographic information is available from OCA.

Reference

Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases., Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ, Eur J Biochem. 2001 Dec;268(24):6625-36. PMID:11737217

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