6kqo

<table><tr><td colspan='2'>[[6kqo]] is a 12 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KQO FirstGlance]. <br>

</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>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6kou|6kou]]</td></tr>

<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=6kqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kqo OCA], [http://pdbe.org/6kqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kqo RCSB], [http://www.ebi.ac.uk/pdbsum/6kqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kqo ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

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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== References ==

[[Category: Chang, Y C]]

[[Category: Chen, C Y]]

[[Category: Huang, C H]]

[[Category: Lin, B L]]

[[Category: Tsai, M D]]

[[Category: Complex]]

[[Category: Isomerase]]