1E5R

Proline 3-hydroxylase (type II) -apo form

Summary for 1E5R

• Entry DOI: 10.2210/pdb1e5r/pdb
• Related: 1E5S
• Descriptor: PROLINE OXIDASE (2 entities in total)
• Functional Keywords: oxidoreductase, oxygenase, 2-oxoglutarate dependent oxygenase
• Biological source: STREPTOMYCES SP.
• Total number of polymer chains: 2
• Total formula weight: 67237.55

Authors

Clifton, I.J.,Hsueh, L.C.,Baldwin, J.E.,Schofield, C.J.,Harlos, K. (deposition date: 2000-07-28, release date: 2001-07-26, Last modification date: 2024-05-08)

Primary citation

Clifton, I.J.,Hsueh, L.C.,Baldwin, J.E.,Harlos, K.,Schofield, C.J.
Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.
Eur.J.Biochem., 268:6625-6636, 2001

PubMed Abstract: 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.

PubMed: 11737217
DOI: 10.1046/j.0014-2956.2001.02617.x

Experimental method

X-RAY DIFFRACTION (2.3 Å)