Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis (CROSBI ID 101597)
Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija
Podaci o odgovornosti
Bučević-Popović, Viljemka ; Pavela-Vrančič, Maja ; Dieckmann, Ralf
engleski
Metal-ion induced conformational changes in alkaline phosphatase from E. coli assessed by limited proteolysis
Alkaline phosphatase (AP) displays significant structural changes during metal-ion binding, supporting cooperative interactions between the subunits of the dimeric enzyme. Here, we present data on the dynamic properties of AP from E. coli, and characterize the structural changes that accompany variations in metal-ion content, combining limited proteolysis and MALDI-TOF mass spectrometry. Limited proteolysis revealed an internal cleavage site at Arg-293, reflecting a position of conformational flexibility supporting subunit communication essential for catalysis. A specific shielding of a region distant from the metal-binding site has been demonstrated, implying transmission of conformational changes, induced by metal-ion binding to the adjacent subunit, across the subunit interface.
Alkaline phosphatase ; metal ion ; conformational change ; limited proteolysis ; MALDI-TOF mass spectrometry
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano
nije evidentirano