8h85: Difference between revisions
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==Trans-3/4-proline-hydroxylase H11 with 3-hydroxyl-proline== | |||
<StructureSection load='8h85' size='340' side='right'caption='[[8h85]], [[Resolution|resolution]] 2.38Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8h85]] 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=8H85 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8H85 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HY3:3-HYDROXYPROLINE'>HY3</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=8h85 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8h85 OCA], [https://pdbe.org/8h85 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8h85 RCSB], [https://www.ebi.ac.uk/pdbsum/8h85 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8h85 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 8h85" 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 3-hydroxyl-proline
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