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7dl0
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 7dl0 is ON HOLD Authors: Description: Category: Unreleased Structures) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The mutant E310G/A314Y of 3,5-DAHDHcca complex with NADPH== |
| + | <StructureSection load='7dl0' size='340' side='right'caption='[[7dl0]], [[Resolution|resolution]] 2.17Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DL0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DL0 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]] 2.17Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=7dl0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dl0 OCA], [https://pdbe.org/7dl0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dl0 RCSB], [https://www.ebi.ac.uk/pdbsum/7dl0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dl0 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Amino acid dehydrogenases (AADHs) have shown considerable potential as biocatalysts in the asymmetric synthesis of chiral amino acids. However, compared to the widely studied alpha-AADHs, limited knowledge is available about beta-AADHs that enable the synthesis of beta-amino acids. Herein, we report the crystal structures of a l-erythro-3,5-diaminohexanoate dehydrogenase and its variants, the only known member of beta-AADH family. Crystal structure analysis, site-directed mutagenesis studies and quantum chemical calculations revealed the differences in the substrate binding and catalytic mechanism from alpha-AADHs. A number of rationally engineered variants were then obtained with improved activity (by 110-800 times) toward various aliphatic beta-amino acids without an enantioselectivity trade-off. Two beta-amino acids were prepared by using the outstanding variants with excellent enantioselectivity (>99 % ee) and high isolated yields (86-87 %). These results provide important insights into the molecular mechanism of 3,5-DAHDH, and establish a solid foundation for further design of beta-AADHs for the asymmetric synthesis of beta-amino acids. | ||
| - | + | Crystal Structures and Catalytic Mechanism of l-erythro-3,5-Diaminohexanoate Dehydrogenase and Rational Engineering for Asymmetric Synthesis of beta-Amino Acids.,Liu N, Wu L, Feng J, Sheng X, Li J, Chen X, Li J, Liu W, Zhou J, Wu Q, Zhu D Angew Chem Int Ed Engl. 2021 Apr 26;60(18):10203-10210. doi:, 10.1002/anie.202017225. Epub 2021 Mar 24. PMID:33624917<ref>PMID:33624917</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7dl0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Liu N]] | ||
| + | [[Category: Wu L]] | ||
| + | [[Category: Zhou JH]] | ||
| + | [[Category: Zhu DM]] | ||
Current revision
The mutant E310G/A314Y of 3,5-DAHDHcca complex with NADPH
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Categories: Large Structures | Liu N | Wu L | Zhou JH | Zhu DM
