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5ywn

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Current revision (10:25, 27 March 2024) (edit) (undo)
 
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<StructureSection load='5ywn' size='340' side='right'caption='[[5ywn]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
<StructureSection load='5ywn' size='340' side='right'caption='[[5ywn]], [[Resolution|resolution]] 2.04&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5ywn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Picst Picst]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YWN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YWN FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5ywn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Scheffersomyces_stipitis_CBS_6054 Scheffersomyces stipitis CBS 6054]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YWN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YWN 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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</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]] 2.039&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GRP3.1, PICST_32463 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=322104 PICST])</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=NAP:NADP+NICOTINAMIDE-ADENINE-DINUCLEOTIDE+PHOSPHATE'>NAP</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Cinnamyl-alcohol_dehydrogenase Cinnamyl-alcohol dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.195 1.1.1.195] </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=5ywn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ywn OCA], [https://pdbe.org/5ywn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ywn RCSB], [https://www.ebi.ac.uk/pdbsum/5ywn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ywn ProSAT]</span></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=5ywn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ywn OCA], [http://pdbe.org/5ywn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ywn RCSB], [http://www.ebi.ac.uk/pdbsum/5ywn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ywn ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/A3LWG4_PICST A3LWG4_PICST]
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Substrate inhibition of enzymes is one of the main obstacles encountered frequently in industrial biocatalysis. Haloketone reductase SsCR was seriously inhibited by substrate 2,2',4'-trichloroacetophenone. In this study, two essential loops were found that have a relationship with substrate binding by conducting X-ray crystal structure analysis. Three key residues were selected from the tips of the loops and substituted with amino acids with lower hydrophobicity to weaken the hydrophobic interactions that bridge the two loops, resulting in a remarkable reduction of substrate inhibition. Among these variants, L211H showed a significant attenuation of substrate inhibition, with a Ki of 16 mM, which was 16 times that of the native enzyme. The kinetic parameter kcat/Km of L211H was 3.1 x 10(3) s(-1) mM(-1), showing the comparable catalytic efficiency to that of the wild-type enzyme (WT). At the substrate loading of 100 mM, the space time yield of variant L211H in asymmetric reduction of the haloketone was 3-fold higher than that of the WT.
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Attenuated substrate inhibition of a haloketone reductase via structure-guided loop engineering.,Shang YP, Chen Q, Li AT, Quan S, Xu JH, Yu HL J Biotechnol. 2020 Jan 20;308:141-147. doi: 10.1016/j.jbiotec.2019.12.011. Epub, 2019 Dec 19. PMID:31866427<ref>PMID:31866427</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 5ywn" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cinnamyl-alcohol dehydrogenase]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Picst]]
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[[Category: Scheffersomyces stipitis CBS 6054]]
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[[Category: Chen, Q]]
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[[Category: Chen Q]]
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[[Category: Shang, Y P]]
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[[Category: Shang YP]]
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[[Category: Xu, J H]]
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[[Category: Xu JH]]
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[[Category: Yu, H L]]
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[[Category: Yu HL]]
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[[Category: Asymmetric reduction]]
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[[Category: Oxidoreductase]]
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[[Category: Reductase]]
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[[Category: Substrate inhibition]]
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Current revision

SsCR_L211H-NADP+

PDB ID 5ywn

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