1e5r: Difference between revisions
New page: left|200px<br /><applet load="1e5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1e5r, resolution 2.3Å" /> '''PROLINE 3-HYDROXYLASE... |
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[[Image:1e5r.jpg|left|200px]]<br /><applet load="1e5r" size=" | [[Image:1e5r.jpg|left|200px]]<br /><applet load="1e5r" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1e5r, resolution 2.3Å" /> | caption="1e5r, resolution 2.3Å" /> | ||
'''PROLINE 3-HYDROXYLASE (TYPE II)-APO FORM'''<br /> | '''PROLINE 3-HYDROXYLASE (TYPE II)-APO FORM'''<br /> | ||
==Overview== | ==Overview== | ||
Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative | 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== | ==About this Structure== | ||
1E5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Streptomyces_sp. Streptomyces sp.]. Full crystallographic information is available from [http:// | 1E5R is a [http://en.wikipedia.org/wiki/Single_protein 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== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Streptomyces sp.]] | [[Category: Streptomyces sp.]] | ||
[[Category: Baldwin, J | [[Category: Baldwin, J E.]] | ||
[[Category: Clifton, I | [[Category: Clifton, I J.]] | ||
[[Category: Harlos, K.]] | [[Category: Harlos, K.]] | ||
[[Category: Hsueh, L | [[Category: Hsueh, L C.]] | ||
[[Category: Schofield, C | [[Category: Schofield, C J.]] | ||
[[Category: 2-oxoglutarate dependent oxygenase]] | [[Category: 2-oxoglutarate dependent oxygenase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:24:08 2008'' | ||
Revision as of 10:24, 21 February 2008
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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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