6y4d: Difference between revisions
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<StructureSection load='6y4d' size='340' side='right'caption='[[6y4d]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='6y4d' size='340' side='right'caption='[[6y4d]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6y4d]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[6y4d]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Zephyranthes_treatiae Zephyranthes treatiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6Y4D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6Y4D FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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=6y4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y4d OCA], [https://pdbe.org/6y4d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6y4d RCSB], [https://www.ebi.ac.uk/pdbsum/6y4d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6y4d ProSAT]</span></td></tr> | |||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Zephyranthes treatiae]] | [[Category: Zephyranthes treatiae]] | ||
[[Category: Mueller | [[Category: Mueller M]] | ||
[[Category: Roth | [[Category: Roth S]] | ||
[[Category: Sautner | [[Category: Sautner V]] | ||
[[Category: Steimle | [[Category: Steimle S]] | ||
[[Category: Tittmann | [[Category: Tittmann K]] | ||
Latest revision as of 16:19, 24 January 2024
Crystal structure of a short-chain dehydrogenase/reductase (SDR) from Zephyranthes treatiae in complex with NADP+Crystal structure of a short-chain dehydrogenase/reductase (SDR) from Zephyranthes treatiae in complex with NADP+
Structural highlights
Publication Abstract from PubMedThe family of NAD(P)H-dependent short-chain dehydrogenases/reductases (SDRs) comprises numerous biocatalysts capable of C=O or C=C reduction. The highly homologous noroxomaritidine reductase (NR) from Narcissus sp. aff. pseudonarcissus and Zt_SDR from Zephyranthes treatiae, however, are SDRs with an extended imine substrate scope. Comparison with a similar SDR from Asparagus officinalis (Ao_SDR) exhibiting keto-reducing activity, yet negligible imine-reducing capability, and mining the Short-Chain Dehydrogenase/Reductase Engineering Database indicated that NR and Zt_SDR possess a unique active-site composition among SDRs. Adapting the active site of Ao_SDR accordingly improved its imine-reducing capability. By applying the same strategy, an unrelated SDR from Methylobacterium sp. 77 (M77_SDR) with distinct keto-reducing activity was engineered into a promiscuous enzyme with imine-reducing activity, thereby confirming that the ability to reduce imines can be rationally introduced into members of the "classical" SDR enzyme family. Thus, members of the SDR family could be a promising starting point for protein approaches to generate new imine-reducing enzymes. Crossing the Border: From Keto- to Imine Reduction in Short-Chain Dehydrogenases/Reductases.,Roth S, Stockinger P, Steff J, Steimle S, Sautner V, Tittmann K, Pleiss J, Muller M Chembiochem. 2020 Sep 14;21(18):2615-2619. doi: 10.1002/cbic.202000233. Epub 2020, Jul 2. PMID:32315494[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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