Ribbon drawing of the rat hexokinase-1 dimer (one monomer is steel blue and the other is green) with bound glucose (yellow) and glucose-6-phosphate (red). Note the two identical domains in each monomer and their associated binding clefts as well as the intervening helical linker. The membrane binding peptide (MBP) is colored copper. See reference below: Mulichak, et al., 1998.
Superpositions of the N-terminal (rHK-In) and C-terminal (rHK-Ic) domains
with each other and with the homologous S. mansoni hexokinase (SHEX) and
the "more primative" yeast hexokinase A (yHK-A).
 A space filling model of the rat hexokinase-1 dimer showing the location of the membrane binding peptide (MBP) on the same side of the molecule. A hypothetical membran plane shows how the MBP might be interacting with the outer mitochondrial membrane. |
References of interest
Mulichak, A. M., Wilson, J. E., Padmanabhan, K., and Garavito, R. M. (1998) "The structure of mammalian hexokinase-1." Nature Struct. Biol. 5, 555-560.
Sebastian, S., Wilson, J. E., Mulichak, A. M., and Garavito, R. M. (1999) "Allosteric regulation of Type I hexokinase: A site-directed mutational study indicating localization of the functional glucose 6-phophate site in the N-terminal half of the enzyme." Arch. Biochem. Biophys. 362, 203-210