View source for 8b26


==Dihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga==
<StructureSection load='8b26' size='340' side='right'caption='[[8b26]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8b26]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Tabernanthe_iboga Tabernanthe iboga]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8B26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B26 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=8b26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b26 OCA], [https://pdbe.org/8b26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b26 RCSB], [https://www.ebi.ac.uk/pdbsum/8b26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b26 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A5B8X8Z0_TABIB A0A5B8X8Z0_TABIB] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Medium-chain alcohol dehydrogenases (ADHs) comprise a highly conserved enzyme family that catalyse the reversible reduction of aldehydes. However, recent discoveries in plant natural product biosynthesis suggest that the catalytic repertoire of ADHs has been expanded. Here we report the crystal structure of dihydroprecondylocarpine acetate synthase (DPAS), an ADH that catalyses the non-canonical 1,4-reduction of an alpha,beta -unsaturated iminium moiety. Comparison with structures of plant-derived ADHs suggest the 1,4-iminium reduction does not require a proton relay or the presence of a catalytic zinc ion in contrast to canonical 1,2-aldehyde reducing ADHs that require the catalytic zinc and a proton relay. Furthermore, ADHs that catalysed 1,2-iminium reduction required the presence of the catalytic zinc and the loss of the proton relay. This suggests how the ADH active site can be modified to perform atypical carbonyl reductions, providing insight into how chemical reactions are diversified in plant metabolism.

Expansion of the Catalytic Repertoire of Alcohol Dehydrogenases in Plant Metabolism.,Langley C, Tatsis E, Hong B, Nakamura Y, Paetz C, Stevenson CE, Basquin J, Lawson DM, Caputi L, O'Connor SE Angew Chem Int Ed Engl. 2022 Oct 5. doi: 10.1002/anie.202210934. PMID:36198083<ref>PMID:36198083</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8b26" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tabernanthe iboga]]
[[Category: Basquin J]]
[[Category: Caputi L]]
[[Category: Langley C]]
[[Category: O'Connor SE]]