1e5s

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{{STRUCTURE_1e5s| PDB=1e5s | SCENE= }}
{{STRUCTURE_1e5s| PDB=1e5s | SCENE= }}
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'''PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM'''
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===PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11737217 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11737217}}
==About this Structure==
==About this Structure==
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[[Category: Schofield, C J.]]
[[Category: Schofield, C J.]]
[[Category: 2-oxoglutarate dependent oxygenase]]
[[Category: 2-oxoglutarate dependent oxygenase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 14:42:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 00:11:44 2008''

Revision as of 21:11, 30 June 2008

Image:1e5s.png

Template:STRUCTURE 1e5s

PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM

Template:ABSTRACT PUBMED 11737217

About this Structure

1E5S 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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