5gwr: Difference between revisions

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'''Unreleased structure'''


The entry 5gwr is ON HOLD
==4-hydroxyisoleucine dehydrogenase complexed with NADH==
<StructureSection load='5gwr' size='340' side='right'caption='[[5gwr]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gwr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GWR 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</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=5gwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gwr OCA], [https://pdbe.org/5gwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gwr RCSB], [https://www.ebi.ac.uk/pdbsum/5gwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gwr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A0K0Q8K4_BACTU A0A0K0Q8K4_BACTU]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Fenugreek is a dietary supplement for anti-aging and human health. (2S,3R,4S)-4-hydroxyisoleucine (4-HIL), which is extracted from fenugreek seeds, is expected to be a promising orally active drug for diabetes and diabetic nephropathy because of its insulinotropic effect. Although several chemical synthesis methods of 4-HIL have been proposed, these methods require multistep reactions to control the stereochemistry of 4-HIL. In this study, we modified the key enzyme 4-HIL dehydrogenase (HILDH) to overcome the biggest limitation in commercial-scale production of 4-HIL. As a result, an effective one-step carbonyl reduction to produce (2S,3R,4S)-4-HIL was successfully accomplished with strict stereoselectivity (&gt;99% de). Mass production of (2S,3R,4S)-4-HIL by our synthetic method could have a significant contribution to the prevention of diabetes, dyslipidemia, and Alzheimer's disease. (120 words/200 words).


Authors: Shi, X., Miyakawa, T., Nakamura, A., Tanokura, M.
Engineering a short-chain dehydrogenase/reductase for the stereoselective production of (2S,3R,4S)-4-hydroxyisoleucine with three asymmetric centers.,Shi X, Miyakawa T, Nakamura A, Hou F, Hibi M, Ogawa J, Kwon Y, Tanokura M Sci Rep. 2017 Oct 20;7(1):13703. doi: 10.1038/s41598-017-13978-w. PMID:29057974<ref>PMID:29057974</ref>


Description: 4-hydroxyisoleucine dehydrogenase complexed with NADH
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Shi, X]]
<div class="pdbe-citations 5gwr" style="background-color:#fffaf0;"></div>
[[Category: Tanokura, M]]
== References ==
[[Category: Miyakawa, T]]
<references/>
[[Category: Nakamura, A]]
__TOC__
</StructureSection>
[[Category: Bacillus thuringiensis]]
[[Category: Large Structures]]
[[Category: Miyakawa T]]
[[Category: Nakamura A]]
[[Category: Shi X]]
[[Category: Tanokura M]]
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