3FGU
Catalytic complex of Human Glucokinase
Summary for 3FGU
| Entry DOI | 10.2210/pdb3fgu/pdb |
| Related | 1V4S 1V4T 3F9M |
| Descriptor | Glucokinase, beta-D-glucopyranose, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (6 entities in total) |
| Functional Keywords | glucokinase, hexokinase iv, atp-binding, diabetes mellitus, disease mutation, glycolysis, kinase, nucleotide-binding, transferase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 53745.94 |
| Authors | Petit, P.,Lagarde, A.,Boutin, J.A.,Ferry, G.,Vuillard, L. (deposition date: 2008-12-08, release date: 2009-12-15, Last modification date: 2023-11-01) |
| Primary citation | Petit, P.,Antoine, M.,Ferry, G.,Boutin, J.A.,Lagarde, A.,Gluais, L.,Vincentelli, R.,Vuillard, L. The active conformation of human glucokinase is not altered by allosteric activators Acta Crystallogr.,Sect.D, 67:929-935, 2011 Cited by PubMed Abstract: Glucokinase (GK) catalyses the formation of glucose 6-phosphate from glucose and ATP. A specific feature of GK amongst hexokinases is that it can cycle between active and inactive conformations as a function of glucose concentration, resulting in a unique positive kinetic cooperativity with glucose, which turns GK into a unique key sensor of glucose metabolism, notably in the pancreas. GK is a target of antidiabetic drugs aimed at the activation of GK activity, leading to insulin secretion. Here, the first structures of a GK-glucose complex without activator, of GK-glucose-AMP-PNP and of GK-glucose-AMP-PNP with a bound activator are reported. All these structures are extremely similar, thus demonstrating that binding of GK activators does not result in conformational changes of the active protein but in stabilization of the active form of GK. PubMed: 22101819DOI: 10.1107/S0907444911036729 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.15 Å) |
Structure validation
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