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5gwt

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==4-hydroxyisoleucine dehydrogenase mutant complexed with NADH and succinate==
==4-hydroxyisoleucine dehydrogenase mutant complexed with NADH and succinate==
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<StructureSection load='5gwt' size='340' side='right' caption='[[5gwt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
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<StructureSection load='5gwt' size='340' side='right'caption='[[5gwt]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5gwt]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GWT FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5gwt]] 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=5GWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GWT FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5gwr|5gwr]], [[5gws|5gws]]</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SIN:SUCCINIC+ACID'>SIN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gwt OCA], [http://pdbe.org/5gwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5gwt RCSB], [http://www.ebi.ac.uk/pdbsum/5gwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5gwt ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5gwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gwt OCA], [https://pdbe.org/5gwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gwt RCSB], [https://www.ebi.ac.uk/pdbsum/5gwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gwt ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/A0A0K0Q8K4_BACTU A0A0K0Q8K4_BACTU]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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).
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5gwt" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Miyakawa, T]]
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[[Category: Bacillus thuringiensis]]
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[[Category: Nakamura, A]]
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[[Category: Large Structures]]
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[[Category: Shi, X]]
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[[Category: Miyakawa T]]
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[[Category: Tanokura, M]]
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[[Category: Nakamura A]]
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[[Category: Dehydrogenase]]
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[[Category: Shi X]]
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[[Category: Nadh-dependent]]
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[[Category: Tanokura M]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]
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[[Category: Short-chain]]
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4-hydroxyisoleucine dehydrogenase mutant complexed with NADH and succinate

PDB ID 5gwt

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