8jhe: Difference between revisions

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-'''Unreleased structure'''
-The entry 8jhe is ON HOLD
+==Hyper-thermostable ancestral L-amino acid oxidase 2 (HTAncLAAO2)==
+<StructureSection load='8jhe' size='340' side='right'caption='[[8jhe]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[8jhe]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8JHE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JHE 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]] 2.201&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=8jhe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jhe OCA], [https://pdbe.org/8jhe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jhe RCSB], [https://www.ebi.ac.uk/pdbsum/8jhe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jhe ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Production of D-amino acids (D-AAs) on a large-scale enables to provide precursors of peptide therapeutics. In this study, we designed a novel L-amino acid oxidase, HTAncLAAO2, by ancestral sequence reconstruction, exhibiting high thermostability and long-term stability. The crystal structure of HTAncLAAO2 was determined at 2.2 A by X-ray crystallography, revealing that the enzyme has an octameric form like a "ninja-star" feature. Enzymatic property analysis demonstrated that HTAncLAAO2 exhibits three-order larger k(cat)/K(m) values towards four L-AAs (L-Phe, L-Leu, L-Met, and L-Ile) than that of L-Trp. Through screening the variants, we obtained the HTAncLAAO2(W220A) variant, which shows a &gt; 6-fold increase in k(cat) value toward L-Trp compared to the original enzyme. This variant applies to synthesizing enantio-pure D-Trp derivatives from L- or rac-forms at a preparative scale. Given its excellent properties, HTAncLAAO2 would be a starting point for designing novel oxidases with high activity toward various amines and AAs.
-Authors: Kawamura, Y., Ishida, C., Miyata, R., Miyata, A., Hayashi, S., Fujinami, D., Ito, S., Nakano, S.
+Structural and functional analysis of hyper-thermostable ancestral L-amino acid oxidase that can convert Trp derivatives to D-forms by chemoenzymatic reaction.,Kawamura Y, Ishida C, Miyata R, Miyata A, Hayashi S, Fujinami D, Ito S, Nakano S Commun Chem. 2023 Sep 22;6(1):200. doi: 10.1038/s42004-023-01005-1. PMID:37737277<ref>PMID:37737277</ref>
-Description: Hyper-thermostable ancestral L-amino acid oxidase 2 (HTAncLAAO2)
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Kawamura, Y]]
+<div class="pdbe-citations 8jhe" style="background-color:#fffaf0;"></div>
-[[Category: Ito, S]]
+== References ==
-[[Category: Nakano, S]]
+<references/>
-[[Category: Miyata, A]]
+__TOC__
-[[Category: Fujinami, D]]
+</StructureSection>
-[[Category: Ishida, C]]
+[[Category: Large Structures]]
-[[Category: Hayashi, S]]
+[[Category: Synthetic construct]]
-[[Category: Miyata, R]]
+[[Category: Fujinami D]]
+[[Category: Hayashi S]]
+[[Category: Ishida C]]
+[[Category: Ito S]]
+[[Category: Kawamura Y]]
+[[Category: Miyata A]]
+[[Category: Miyata R]]
+[[Category: Nakano S]]