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8h7v
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Trans-3/4-proline-hydroxylase H11 with AKG== | |
| + | <StructureSection load='8h7v' size='340' side='right'caption='[[8h7v]], [[Resolution|resolution]] 1.97Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8h7v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium_esnapd13 Uncultured bacterium esnapd13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8H7V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H7V FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.97Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AKG:2-OXOGLUTARIC+ACID'>AKG</scene>, <scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></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=8h7v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h7v OCA], [https://pdbe.org/8h7v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h7v RCSB], [https://www.ebi.ac.uk/pdbsum/8h7v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h7v ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/S5TUM1_9BACT S5TUM1_9BACT] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | L-Proline hydroxylase is a member of the non-heme Fe(2+)/alpha-ketoglutarate (AKG)-dependent hydroxylase family that catalyzes the reaction from L-proline to hydroxy-L-proline, which is widely used in drug synthesis, biochemistry, food supplementation and cosmetic industries. Here, the first crystal structure of L-proline trans-hydroxylase and its complexes with substrate and product are reported, which reveal the structural basis of trans-cis proline hydroxylation selectivity. Structure comparison with other AKG-dependent hydroxylases identifies conserved amino acid residues, which may serve as signatures of in-line or off-line AKG binding modes in the AKG-dependent enzyme family. | ||
| - | + | Structures of L-proline trans-hydroxylase reveal the catalytic specificity and provide deeper insight into AKG-dependent hydroxylation.,Hu X, Huang X, Liu J, Zheng P, Gong W, Yang L Acta Crystallogr D Struct Biol. 2023 Apr 1;79(Pt 4):318-325. doi: , 10.1107/S2059798323001936. Epub 2023 Mar 28. PMID:36974966<ref>PMID:36974966</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 8h7v" style="background-color:#fffaf0;"></div> |
| - | [[Category: Gong | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Uncultured bacterium esnapd13]] | ||
| + | [[Category: Gong WM]] | ||
| + | [[Category: Hu XY]] | ||
Current revision
Trans-3/4-proline-hydroxylase H11 with AKG
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