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6y4d
From Proteopedia
(Difference between revisions)
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==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+== | ||
| - | <StructureSection load='6y4d' size='340' side='right'caption='[[6y4d]]' scene=''> | + | <StructureSection load='6y4d' size='340' side='right'caption='[[6y4d]], [[Resolution|resolution]] 2.10Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>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 [http://proteopedia.org/fgij/fg.htm?mol=6Y4D FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6y4d]] is a 2 chain structure with sequence from [http://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 [http://proteopedia.org/fgij/fg.htm?mol=6Y4D FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y4d OCA], [http://pdbe.org/6y4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y4d RCSB], [http://www.ebi.ac.uk/pdbsum/6y4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y4d ProSAT]</span></td></tr> | + | </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> |
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6y4d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6y4d OCA], [http://pdbe.org/6y4d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6y4d RCSB], [http://www.ebi.ac.uk/pdbsum/6y4d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6y4d ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 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<ref>PMID:32315494</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6y4d" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Mueller M]] | + | [[Category: Zephyranthes treatiae]] |
| - | [[Category: Roth S]] | + | [[Category: Mueller, M]] |
| - | [[Category: Sautner V]] | + | [[Category: Roth, S]] |
| - | [[Category: Steimle S]] | + | [[Category: Sautner, V]] |
| - | [[Category: Tittmann K]] | + | [[Category: Steimle, S]] |
| + | [[Category: Tittmann, K]] | ||
| + | [[Category: Asymmetric reduction]] | ||
| + | [[Category: Biocatalysis]] | ||
| + | [[Category: Complex]] | ||
| + | [[Category: Imine reduction]] | ||
| + | [[Category: Mutagenesis]] | ||
| + | [[Category: Oxidoreductase]] | ||
| + | [[Category: Rational design]] | ||
| + | [[Category: Short-chain dehydrogenase/reductase]] | ||
Revision as of 11:31, 23 September 2020
Crystal structure of a short-chain dehydrogenase/reductase (SDR) from Zephyranthes treatiae in complex with NADP+
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