8b25: Difference between revisions
New page: '''Unreleased structure''' The entry 8b25 is ON HOLD Authors: Langley, C., Basquin, J., Caputi, L., O''Connor, S.E. Description: Dihydroprecondylocarpine acetate synthase 2 from Tabern... |
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==Dihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga - stemmadenine acetate bound structure== | |||
<StructureSection load='8b25' size='340' side='right'caption='[[8b25]], [[Resolution|resolution]] 2.24Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8b25]] 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=8B25 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8B25 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]] 2.24Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=OSO:stemmadenine+acetate'>OSO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <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=8b25 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8b25 OCA], [https://pdbe.org/8b25 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8b25 RCSB], [https://www.ebi.ac.uk/pdbsum/8b25 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8b25 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 8b25" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Langley | <references/> | ||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Tabernanthe iboga]] | |||
[[Category: Basquin J]] | |||
[[Category: Caputi L]] | |||
[[Category: Langley C]] | |||
[[Category: O'Connor SE]] | |||
Latest revision as of 16:38, 1 February 2024
Dihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga - stemmadenine acetate bound structureDihydroprecondylocarpine acetate synthase 2 from Tabernanthe iboga - stemmadenine acetate bound structure
Structural highlights
FunctionPublication Abstract from PubMedMedium-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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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