6p2i
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Acyclic imino acid reductase (Bsp5) in complex with NADPH and D-Arg== | |
| + | <StructureSection load='6p2i' size='340' side='right'caption='[[6p2i]], [[Resolution|resolution]] 1.63Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6p2i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_sp._5mfcol3.1 Bacillus sp. 5mfcol3.1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6P2I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6P2I 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]] 1.63Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAR:D-ARGININE'>DAR</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=6p2i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6p2i OCA], [https://pdbe.org/6p2i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6p2i RCSB], [https://www.ebi.ac.uk/pdbsum/6p2i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6p2i ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A1I4FUG4_9BACI A0A1I4FUG4_9BACI] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Acyclic imines are unstable in aqueous conditions. For this reason, known imine reductases, which enable the synthesis of chiral amines, mainly intercept stable cyclic imines. Here we report the detailed biochemical and structural characterization of Bsp5, an imino acid reductase from the D-2-hydroxyacid dehydrogenase family that reduces acyclic imino acids produced in situ by a partner oxidase. We determine a 1.6 A resolution structure of Bsp5 in complex with D-arginine and coenzyme NADPH. Combined with mutagenesis work, our study reveals the minimal structural constraints for its biosynthetic activity. Furthermore, we demonstrate that Bsp5 can intercept more complex products from an alternate oxidase partner, suggesting that this oxidase-imino acid reductase pair could be evolved for biocatalytic conversion of L-amino acids to D-amino acids. | ||
| - | + | An Asymmetric Reductase that Intercepts Acyclic Imino Acids Produced In Situ by a Partner Oxidase.,Guo J, Higgins MA, Daniel-Ivad P, Ryan KS J Am Chem Soc. 2019 Jul 12. doi: 10.1021/jacs.9b03307. PMID:31298853<ref>PMID:31298853</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6p2i" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus sp. 5mfcol3 1]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Daniel-Ivad P]] | ||
| + | [[Category: Guo J]] | ||
| + | [[Category: Higgins MA]] | ||
| + | [[Category: Ryan KS]] | ||
Current revision
Acyclic imino acid reductase (Bsp5) in complex with NADPH and D-Arg
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