1e5r
From Proteopedia
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| - | [[Image:1e5r.jpg|left|200px]] | + | [[Image:1e5r.jpg|left|200px]] |
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| - | '''PROLINE 3-HYDROXYLASE (TYPE II)-APO FORM''' | + | {{Structure |
| + | |PDB= 1e5r |SIZE=350|CAPTION= <scene name='initialview01'>1e5r</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''PROLINE 3-HYDROXYLASE (TYPE II)-APO FORM''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1E5R is a [ | + | 1E5R is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5R OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11737217 11737217] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
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[[Category: 2-oxoglutarate dependent oxygenase]] | [[Category: 2-oxoglutarate dependent oxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:16 2008'' |
Revision as of 08:50, 20 March 2008
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| , resolution 2.3Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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