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6agz

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Current revision (10:31, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6agz' size='340' side='right'caption='[[6agz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='6agz' size='340' side='right'caption='[[6agz]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6agz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AGZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6AGZ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6agz]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Pichia Pichia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6AGZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6AGZ 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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</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&#8491;</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=6agz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agz OCA], [http://pdbe.org/6agz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6agz RCSB], [http://www.ebi.ac.uk/pdbsum/6agz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6agz ProSAT]</span></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=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene></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=6agz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6agz OCA], [https://pdbe.org/6agz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6agz RCSB], [https://www.ebi.ac.uk/pdbsum/6agz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6agz ProSAT]</span></td></tr>
</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/A0A5H1ZR30_9ASCO A0A5H1ZR30_9ASCO]
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Old yellow enzymes (OYEs) are potential targets of protein engineering for useful biocatalysts because of their excellent asymmetric reductions of enone compounds. Two OYEs from different yeast strains, Candida macedoniensis AKU4588 OYE (CmOYE) and Pichia sp. AKU4542 OYE (PsOYE), have a sequence identity of 46%, but show different substrate preferences; PsOYE shows 3.4-fold and 39-fold higher catalytic activities than CmOYE toward ketoisophorone and (4S)-phorenol, respectively. To gain insights into structural basis of their different substrate preferences, we have solved a crystal structure of PsOYE, and compared its catalytic site structure with that of CmOYE, revealing the catalytic pocket of PsOYE is wider than that of CmOYE due to different positions of Phe(246) (PsOYE)/Phe(250) (CmOYE) in static Loop 5. This study shows a significance of 3D structural information to explain the different substrate preferences of yeast OYEs which cannot be understood from their amino acid sequences. Abbreviations: OYE: Old yellow enzymes, CmOYE: Candida macedoniensis AKU4588 OYE, PsOYE: Pichia sp. AKU4542 OYE.
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Structural basis of different substrate preferences of two old yellow enzymes from yeasts in the asymmetric reduction of enone compounds.,Horita S, Kataoka M, Kitamura N, Miyakawa T, Ohtsuka J, Maejima Y, Shimomura K, Nagata K, Shimizu S, Tanokura M Biosci Biotechnol Biochem. 2019 Mar;83(3):456-462. doi:, 10.1080/09168451.2018.1543014. Epub 2018 Nov 16. PMID:30445889<ref>PMID:30445889</ref>
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==See Also==
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*[[NADPH dehydrogenase|NADPH dehydrogenase]]
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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 6agz" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Horita, S]]
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[[Category: Pichia]]
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[[Category: Kataoka, M]]
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[[Category: Horita S]]
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[[Category: Kitamura, N]]
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[[Category: Kataoka M]]
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[[Category: Miyakawa, T]]
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[[Category: Kitamura N]]
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[[Category: Nagata, K]]
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[[Category: Miyakawa T]]
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[[Category: Nakagawa, T]]
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[[Category: Nagata K]]
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[[Category: Ohtsuka, J]]
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[[Category: Nakagawa T]]
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[[Category: Shimizu, S]]
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[[Category: Ohtsuka J]]
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[[Category: Tanokura, M]]
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[[Category: Shimizu S]]
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[[Category: Dehydrogenase]]
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[[Category: Tanokura M]]
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[[Category: Flavoprotein]]
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[[Category: Oxidoreductase]]
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[[Category: Tim barrel motif]]
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Current revision

Crystal structure of Old Yellow Enzyme from Pichia sp. AKU4542

PDB ID 6agz

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