View source for 4bnp


==3D structure of E. coli Isocitrate Dehydrogenase K100M mutant in complex with isocitrate and magnesium(II)==
<StructureSection load='4bnp' size='340' side='right'caption='[[4bnp]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4bnp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BNP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BNP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ICT:ISOCITRIC+ACID'>ICT</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Isocitrate_dehydrogenase_(NADP(+)) Isocitrate dehydrogenase (NADP(+))], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.42 1.1.1.42] </span></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=4bnp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bnp OCA], [http://pdbe.org/4bnp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bnp RCSB], [http://www.ebi.ac.uk/pdbsum/4bnp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bnp ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
An active site lysine essential to catalysis in isocitrate dehydrogenase (IDH) is absent from related enzymes. As all family members catalyze the same oxidative beta-decarboxylation at the (2R)-malate core common to their substrates, it seems odd that an amino acid essential to one is not found in all. Ordinarily, hydride transfer to a nicotinamide C4 neutralizes the positive charge at N1 directly. In IDH, the negatively charged C4-carboxylate of isocitrate stabilizes the ground state positive charge on the adjacent nicotinamide N1, opposing hydride transfer. The critical lysine is poised to stabilize-and perhaps even protonate-an oxyanion formed on the nicotinamide 3-carboxamide, thereby enabling the hydride to be transferred while the positive charge at N1 is maintained. IDH might catalyze the same overall reaction as other family members, but dehydrogenation proceeds through a distinct, though related, transition state. Partial activation of lysine mutants by K+ and NH4 + represents a throwback to the primordial state of the first promiscuous substrate family member.

Evolution of a Transition State: Role of Lys100 in the Active Site of Isocitrate Dehydrogenase.,Miller SP, Goncalves S, Matias PM, Dean AM Chembiochem. 2014 May 2. doi: 10.1002/cbic.201400040. PMID:24797066<ref>PMID:24797066</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4bnp" style="background-color:#fffaf0;"></div>

==See Also==
*[[Isocitrate dehydrogenase|Isocitrate dehydrogenase]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Ecoli]]
[[Category: Large Structures]]
[[Category: Dean, A M]]
[[Category: Goncalves, S]]
[[Category: Matias, P M]]
[[Category: Miller, S P]]
[[Category: Oxidative beta-decarboxylation]]
[[Category: Oxidoreductase]]