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5yeq

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'''Unreleased structure'''
 
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The entry 5yeq is ON HOLD until Paper Publication
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==The structure of Sac-KARI protein==
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<StructureSection load='5yeq' size='340' side='right' caption='[[5yeq]], [[Resolution|resolution]] 1.75&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5yeq]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YEQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YEQ 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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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/Ketol-acid_reductoisomerase Ketol-acid reductoisomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.86 1.1.1.86] </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=5yeq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yeq OCA], [http://pdbe.org/5yeq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5yeq RCSB], [http://www.ebi.ac.uk/pdbsum/5yeq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5yeq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/A0A0U3H6N8_9CREN A0A0U3H6N8_9CREN]] Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate.[HAMAP-Rule:MF_00435]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Ketol-acid reductoisomerase (KARI) is a bifunctional enzyme in the second step of branched-chain amino acids biosynthetic pathway. Most KARIs prefer NADPH as a cofactor. However, KARI with a preference for NADH is desirable in industrial applications including anaerobic fermentation for the production of branched-chain amino acids or biofuels. Here, we characterize a thermoacidophilic archaeal Sac-KARI from Sulfolobus acidocaldarius and present its crystal structure at a 1.75-A resolution. By comparison with other holo-KARI structures, one sulphate ion is observed in each binding site for the 2'-phosphate of NADPH, implicating its NADPH preference. Sac-KARI has very high affinity for NADPH and NADH, with K M values of 0.4 muM for NADPH and 6.0 muM for NADH, suggesting that both are good cofactors at low concentrations although NADPH is favoured over NADH. Furthermore, Sac-KARI can catalyze 2(S)-acetolactate (2S-AL) with either cofactor from 25 to 60 degrees C, but the enzyme has higher activity by using NADPH. In addition, the catalytic activity of Sac-KARI increases significantly with elevated temperatures and reaches an optimum at 60 degrees C. Bi-cofactor utilization and the thermoactivity of Sac-KARI make it a potential candidate for use in metabolic engineering or industrial applications under anaerobic or harsh conditions.
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Authors: Ko, T.P., Chen, C.Y., Lin, K.F., Lin, B.L., Huang, C.H., Chiang, C.H., Horng, J.C., Tsai, M.D.
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NADH/NADPH bi-cofactor-utilizing and thermoactive ketol-acid reductoisomerase from Sulfolobus acidocaldarius.,Chen CY, Ko TP, Lin KF, Lin BL, Huang CH, Chiang CH, Horng JC Sci Rep. 2018 May 8;8(1):7176. doi: 10.1038/s41598-018-25361-4. PMID:29739976<ref>PMID:29739976</ref>
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Description: The structure of Sac-KARI protein
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Ko, T.P]]
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<div class="pdbe-citations 5yeq" style="background-color:#fffaf0;"></div>
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[[Category: Lin, B.L]]
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== References ==
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[[Category: Huang, C.H]]
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<references/>
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[[Category: Horng, J.C]]
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__TOC__
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[[Category: Lin, K.F]]
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</StructureSection>
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[[Category: Chen, C.Y]]
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[[Category: Ketol-acid reductoisomerase]]
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[[Category: Tsai, M.D]]
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[[Category: Chen, C Y]]
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[[Category: Chiang, C.H]]
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[[Category: Chiang, C H]]
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[[Category: Horng, J C]]
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[[Category: Huang, C H]]
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[[Category: Ko, T P]]
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[[Category: Lin, B L]]
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[[Category: Lin, K F]]
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[[Category: Tsai, M D]]
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[[Category: Acid tolerant enzyme]]
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[[Category: Ahir]]
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[[Category: Bcaa]]
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[[Category: Biofuel]]
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[[Category: Branched-chain amino acid]]
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[[Category: Isomerase]]
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[[Category: Knot domain]]
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[[Category: Metal ion cofactor]]
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[[Category: Nadh]]
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[[Category: Nadph]]
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[[Category: Reductase]]

Revision as of 07:09, 4 July 2018

The structure of Sac-KARI protein

5yeq, resolution 1.75Å

Drag the structure with the mouse to rotate

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