This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
8h81
From Proteopedia
(Difference between revisions)
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Trans-3/4-proline-hydroxylase H11 with 4-Hydroxyl-proline== | |
| + | <StructureSection load='8h81' size='340' side='right'caption='[[8h81]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8h81]] is a 1 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=8H81 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H81 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HYP:4-HYDROXYPROLINE'>HYP</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=8h81 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h81 OCA], [https://pdbe.org/8h81 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h81 RCSB], [https://www.ebi.ac.uk/pdbsum/8h81 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h81 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: Gong | + | <div class="pdbe-citations 8h81" style="background-color:#fffaf0;"></div> |
| - | [[Category: Hu | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Uncultured bacterium esnapd13]] | ||
| + | [[Category: Gong WM]] | ||
| + | [[Category: Hu XY]] | ||
Revision as of 09:29, 19 April 2023
Trans-3/4-proline-hydroxylase H11 with 4-Hydroxyl-proline
| |||||||||||
