4p69

Acek (D477A) ICDH complex

spinqualitylabelsall models 4p69, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4p69 is a 4 chain structure with sequence from Escherichia coli K-12 and Escherichia coli O157:H7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.3Å Ligands: ADP, AMP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Isocitrate dehydrogenase 3D structures Isocitrate dehydrogenase kinase/phosphatase

Proteopedia Page Contributors and Editors (what is this?)

OCA