4p69
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Acek (D477A) ICDH complex== | |
| + | <StructureSection load='4p69' size='340' side='right'caption='[[4p69]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4p69]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [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=4P69 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4P69 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</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></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=4p69 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4p69 OCA], [https://pdbe.org/4p69 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4p69 RCSB], [https://www.ebi.ac.uk/pdbsum/4p69 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4p69 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. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | We have revealed that bifunctional AceK kinase/phosphatase utilizes a stepwise addition-elimination mechanism in its dephosphorylation reaction. This work explains how AceK enables opposite kinase and phosphatase activities with Asp477 and a single Mg(2+) ion. | ||
| - | + | The phosphatase mechanism of bifunctional kinase/phosphatase AceK.,Wang S, Shen Q, Chen G, Zheng J, Tan H, Jia Z Chem Commun (Camb). 2014 Nov 25;50(91):14117-20. doi: 10.1039/c4cc05375c. PMID:25272278<ref>PMID:25272278</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4p69" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Isocitrate dehydrogenase 3D structures|Isocitrate dehydrogenase 3D structures]] | ||
| + | *[[Isocitrate dehydrogenase kinase/phosphatase|Isocitrate dehydrogenase kinase/phosphatase]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Escherichia coli O157:H7]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Jimin Z]] | ||
| + | [[Category: Nan W]] | ||
| + | [[Category: Shu W]] | ||
| + | [[Category: Zongchao J]] | ||
Current revision
Acek (D477A) ICDH complex
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