3lc6
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3lc6.jpg|left|200px]] | ||
| - | < | + | ==The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli== |
| - | + | <StructureSection load='3lc6' size='340' side='right'caption='[[3lc6]], [[Resolution|resolution]] 3.10Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | or | + | <table><tr><td colspan='2'>[[3lc6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_O157:H7 Escherichia coli O157:H7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LC6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LC6 FirstGlance]. <br> |
| - | or | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.1Å</td></tr> |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AMP:ADENOSINE+MONOPHOSPHATE'>AMP</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'>[https://proteopedia.org/fgij/fg.htm?mol=3lc6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lc6 OCA], [https://pdbe.org/3lc6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lc6 RCSB], [https://www.ebi.ac.uk/pdbsum/3lc6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lc6 ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ACEK_ECO57 ACEK_ECO57] Bifunctional enzyme which can phosphorylate or dephosphorylate isocitrate dehydrogenase (IDH) on a specific serine residue. This is a regulatory mechanism which enables bacteria to bypass the Krebs cycle via the glyoxylate shunt in response to the source of carbon. When bacteria are grown on glucose, IDH is fully active and unphosphorylated, but when grown on acetate or ethanol, the activity of IDH declines drastically concomitant with its phosphorylation. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/lc/3lc6_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3lc6 ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| - | == | + | ==See Also== |
| - | + | *[[Isocitrate dehydrogenase kinase/phosphatase|Isocitrate dehydrogenase kinase/phosphatase]] | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | [[Category: Escherichia coli O157:H7]] | |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Jia Z]] | |
| - | + | [[Category: Zheng J]] | |
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Current revision
The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli
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