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1e5s

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[[Image:1e5s.gif|left|200px]]
 
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{{Structure
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==Proline 3-hydroxylase (type II) - Iron form==
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|PDB= 1e5s |SIZE=350|CAPTION= <scene name='initialview01'>1e5s</scene>, resolution 2.40&Aring;
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<StructureSection load='1e5s' size='340' side='right'caption='[[1e5s]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
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<table><tr><td colspan='2'>[[1e5s]] 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=1E5S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E5S FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE2:FE+(II)+ION'>FE2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1e5s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e5s OCA], [https://pdbe.org/1e5s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e5s RCSB], [https://www.ebi.ac.uk/pdbsum/1e5s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e5s ProSAT]</span></td></tr>
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</table>
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'''PROLINE 3-HYDROXYLASE (TYPE II)-IRON FORM'''
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== Function ==
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[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]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e5/1e5s_consurf.spt"</scriptWhenChecked>
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1E5S 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=1E5S OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1e5s ConSurf].
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[[Category: Single protein]]
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<div style="clear:both"></div>
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[[Category: Streptomyces sp.]]
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__TOC__
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[[Category: Baldwin, J E.]]
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</StructureSection>
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[[Category: Clifton, I J.]]
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[[Category: Large Structures]]
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[[Category: Harlos, K.]]
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[[Category: Streptomyces sp. TH1]]
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[[Category: Hsueh, L C.]]
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[[Category: Baldwin JE]]
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[[Category: Schofield, C J.]]
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[[Category: Clifton IJ]]
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[[Category: FE2]]
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[[Category: Harlos K]]
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[[Category: SO4]]
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[[Category: Hsueh LC]]
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[[Category: 2-oxoglutarate dependent oxygenase]]
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[[Category: Schofield CJ]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:50:10 2008''
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Current revision

Proline 3-hydroxylase (type II) - Iron form

PDB ID 1e5s

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