tailieunhanh - Báo cáo khoa học: Binding of ATP at the active site of human pancreatic glucokinase – nucleotide-induced conformational changes with possible implications for its kinetic cooperativity

Glucokinase (GK) is the central player in glucose-stimulated insulin release from pancreatic b-cells, and catalytic activation by a-D-glucose binding has a key regulatory function. Whereas the mechanism of this activation is well understood, on the basis of crystal structures of human GK, there are no similar structural data on ATP binding to the ligand-free enzyme and how it affects its conformation. | IFEBS Journal Binding of ATP at the active site of human pancreatic glucokinase - nucleotide-induced conformational changes with possible implications for its kinetic cooperativity Janne Molnes1 2 3 Knut Teigen3 Ingvild Aukrust1 2 3 Lise Bj0rkhaug2 4 Oddmund S0vik2 Torgeir Flatmark3 and Pal Rasmus Nj0lstad1 2 1 Department of Pediatrics Haukeland University Hospital Bergen Norway 2 Department of ClinicalMedicine University of Bergen Norway 3 Department of Biomedicine University of Bergen Norway 4 Center for MedicalGenetics and Molecular Medicine Haukeland University Hospital Norway Keywords ATP binding catalytic mechanism GCK maturity onset diabetes of the young GCK-MODY glucokinase kinetic cooperativity Correspondence T. Flatmark Department of Biomedicine University of Bergen N-5009 Bergen Norway Fax 47 55586360 Tel 47 55586428 E-mail Note The atomic coordinates of the molecular dynamics simulated structural models are available from Received 7 April 2011 revised 20 April 2011 accepted 4 May 2011 doi Glucokinase GK is the central player in glucose-stimulated insulin release from pancreatic b-cells and catalytic activation by a-D-glucose binding has a key regulatory function. Whereas the mechanism of this activation is well understood on the basis of crystal structures of human GK there are no similar structural data on ATP binding to the ligand-free enzyme and how it affects its conformation. Here we report on a conformational change induced by the binding of adenine nucleotides to human pancreatic GK as determined by intrinsic tryptophan fluorescence using the catalytically inactive mutant form T228M to correct for the inner filter effect. Adeno-sine-5 - b y-imido triphosphate and ATP bind to the wild-type enzyme with apparent L ligand concentration at half-maximal effect values of mM and mM respectively. The change in protein conformation was further

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