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| | <StructureSection load='1e5r' size='340' side='right'caption='[[1e5r]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='1e5r' size='340' side='right'caption='[[1e5r]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e5r]] is a 2 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E5R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e5r]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._TH1 Streptomyces sp. TH1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5R FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1e5s|1e5s]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1e5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5r OCA], [http://pdbe.org/1e5r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e5r RCSB], [http://www.ebi.ac.uk/pdbsum/1e5r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5r ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5r OCA], [https://pdbe.org/1e5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5r RCSB], [https://www.ebi.ac.uk/pdbsum/1e5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5r ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/P3H2_STRSQ P3H2_STRSQ]] Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).[PDB:1E5R] | + | [https://www.uniprot.org/uniprot/P3H2_STRSQ P3H2_STRSQ] Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).[PDB:1E5R] |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Streptomyces sp]] | + | [[Category: Streptomyces sp. TH1]] |
| - | [[Category: Baldwin, J E]] | + | [[Category: Baldwin JE]] |
| - | [[Category: Clifton, I J]] | + | [[Category: Clifton IJ]] |
| - | [[Category: Harlos, K]] | + | [[Category: Harlos K]] |
| - | [[Category: Hsueh, L C]] | + | [[Category: Hsueh LC]] |
| - | [[Category: Schofield, C J]] | + | [[Category: Schofield CJ]] |
| - | [[Category: 2-oxoglutarate dependent oxygenase]]
| + | |
| - | [[Category: Oxidoreductase]]
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| - | [[Category: Oxygenase]]
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| Structural highlights
Function
P3H2_STRSQ Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-3-hydroxy-L-proline (cis-3-Hyp).[PDB:1E5R]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Clifton IJ, Hsueh LC, Baldwin JE, Harlos K, Schofield CJ. Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases. Eur J Biochem. 2001 Dec;268(24):6625-36. PMID:11737217
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