1e5s
From Proteopedia
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|PDB= 1e5s |SIZE=350|CAPTION= <scene name='initialview01'>1e5s</scene>, resolution 2.40Å | |PDB= 1e5s |SIZE=350|CAPTION= <scene name='initialview01'>1e5s</scene>, resolution 2.40Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> | + | |LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5s OCA], [http://www.ebi.ac.uk/pdbsum/1e5s PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1e5s RCSB]</span> | ||
}} | }} | ||
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[[Category: Hsueh, L C.]] | [[Category: Hsueh, L C.]] | ||
[[Category: Schofield, C J.]] | [[Category: Schofield, C J.]] | ||
| - | [[Category: FE2]] | ||
| - | [[Category: SO4]] | ||
[[Category: 2-oxoglutarate dependent oxygenase]] | [[Category: 2-oxoglutarate dependent oxygenase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:55:47 2008'' |
Revision as of 16:55, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
PROLINE 3-HYDROXYLASE (TYPE II)-IRON 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
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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