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6kqj

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Current revision (10:43, 27 March 2024) (edit) (undo)
 
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<StructureSection load='6kqj' size='340' side='right'caption='[[6kqj]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
<StructureSection load='6kqj' size='340' side='right'caption='[[6kqj]], [[Resolution|resolution]] 2.54&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6kqj]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KQJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6kqj]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KQJ 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=9TY:cyclopropane-1,1-dicarboxylic+acid'>9TY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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">Electron Microscopy, [[Resolution|Resolution]] 2.54&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6kou|6kou]]</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=9TY:cyclopropane-1,1-dicarboxylic+acid'>9TY</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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=6kqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqj OCA], [http://pdbe.org/6kqj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kqj RCSB], [http://www.ebi.ac.uk/pdbsum/6kqj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqj 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=6kqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqj OCA], [https://pdbe.org/6kqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kqj RCSB], [https://www.ebi.ac.uk/pdbsum/6kqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqj 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/ILVC2_SACS2 ILVC2_SACS2]
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Protein functions are temperature-dependent, but protein structures are usually solved at a single (often low) temperature because of limitations on the conditions of crystal growth or protein vitrification. Here we demonstrate the feasibility of solving cryo-EM structures of proteins vitrified at high temperatures, solve 12 structures of an archaeal ketol-acid reductoisomerase (KARI) vitrified at 4-70 degrees C, and show that structures of both the Mg(2+) form (KARI:2Mg(2+)) and its ternary complex (KARI:2Mg(2+):NADH:inhibitor) are temperature-dependent in correlation with the temperature dependence of enzyme activity. Furthermore, structural analyses led to dissection of the induced-fit mechanism into ligand-induced and temperature-induced effects and to capture of temperature-resolved intermediates of the temperature-induced conformational change. The results also suggest that it is preferable to solve cryo-EM structures of protein complexes at functional temperatures. These studies should greatly expand the landscapes of protein structure-function relationships and enhance the mechanistic analysis of enzymatic functions.
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Temperature-Resolved Cryo-EM Uncovers Structural Bases of Temperature-Dependent Enzyme Functions.,Chen CY, Chang YC, Lin BL, Huang CH, Tsai MD J Am Chem Soc. 2019 Dec 26;141(51):19983-19987. doi: 10.1021/jacs.9b10687. Epub, 2019 Dec 16. PMID:31829582<ref>PMID:31829582</ref>
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==See Also==
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*[[Ketol-acid reductoisomerase 3D structures|Ketol-acid reductoisomerase 3D structures]]
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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 6kqj" 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: Chang, Y C]]
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[[Category: Saccharolobus solfataricus]]
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[[Category: Chen, C Y]]
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[[Category: Chang YC]]
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[[Category: Huang, C H]]
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[[Category: Chen CY]]
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[[Category: Lin, B L]]
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[[Category: Huang CH]]
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[[Category: Tsai, M D]]
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[[Category: Lin BL]]
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[[Category: Complex]]
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[[Category: Tsai MD]]
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[[Category: Isomerase]]
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Current revision

309 K cryoEM structure of Sso-KARI in complex with Mg2+, NADH and CPD

PDB ID 6kqj

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