6jd2: Difference between revisions
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<StructureSection load='6jd2' size='340' side='right'caption='[[6jd2]], [[Resolution|resolution]] 2.53Å' scene=''> | <StructureSection load='6jd2' size='340' side='right'caption='[[6jd2]], [[Resolution|resolution]] 2.53Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jd2]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JD2 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6jd2]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus_P2 Saccharolobus solfataricus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JD2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JD2 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.53Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6jd2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jd2 OCA], [https://pdbe.org/6jd2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jd2 RCSB], [https://www.ebi.ac.uk/pdbsum/6jd2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jd2 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/ILVC2_SACS2 ILVC2_SACS2] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6jd2" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6jd2" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Ketol-acid reductoisomerase 3D structures|Ketol-acid reductoisomerase 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chang | [[Category: Saccharolobus solfataricus P2]] | ||
[[Category: Chen | [[Category: Chang YC]] | ||
[[Category: Hsieh | [[Category: Chen CY]] | ||
[[Category: Huang | [[Category: Hsieh DL]] | ||
[[Category: Ko | [[Category: Huang CH]] | ||
[[Category: Lin | [[Category: Ko TP]] | ||
[[Category: Lin | [[Category: Lin BL]] | ||
[[Category: Tsai | [[Category: Lin KF]] | ||
[[Category: Tsai MD]] | |||
Latest revision as of 13:06, 22 November 2023
Crystal structure of Sulfolobus solfataricus ketol-acid reductoisomerase (Sso-KARI) in complex with Mg2+ at pH8.5Crystal structure of Sulfolobus solfataricus ketol-acid reductoisomerase (Sso-KARI) in complex with Mg2+ at pH8.5
Structural highlights
FunctionPublication Abstract from PubMedWhile cryo-EM is revolutionizing structural biology, its impact on enzymology is yet to be fully demonstrated. The ketol-acid reductoisomerase (KARI) catalyzes conversion of (2 S)-acetolactate or (2 S)-aceto-2-hydroxybutyrate to 2,3-dihydroxy-3-alkylbutyrate. We found that KARI from archaea Sulfolobus solfataricus (Sso-KARI) is unusual in being a dodecamer, bispecific to NADH and NADPH, and losing activity above pH 7.8. While crystals were obtainable only at pH 8.5, cryo-EM structures were solved at pH 7.5 and 8.5 for Sso-KARI:2Mg(2+). The results showed that the distances of the two catalytic Mg(2+) ions are lengthened in both structures at pH 8.5. We next solved cryo-EM structures of two Sso-KARI complexes, with NADH+inhibitor and NADPH+inhibitor at pH 7.5, which indicate that the bispecificity can be attributed to a unique asparagine at the cofactor binding loop. Unexpectedly, Sso-KARI also differs from other KARI enzymes in lacking "induced-fit", reflecting structural rigidity. Thus, cryo-EM is powerful for structural and mechanistic enzymology. Use of Cryo-EM To Uncover Structural Bases of pH Effect and Cofactor Bispecificity of Ketol-Acid Reductoisomerase.,Chen CY, Chang YC, Lin BL, Lin KF, Huang CH, Hsieh DL, Ko TP, Tsai MD J Am Chem Soc. 2019 Apr 2. doi: 10.1021/jacs.9b01354. PMID:30921515[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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