Compartmentation of proteins in cells is important to proper cell function,
interactions of F-actin and glycolytic enzymes is one mechanism by which g
lycolytic enzymes can compartment. Brownian dynamics (BD) simulations of th
e binding of the muscle form of the glycolytic enzyme fructose-1,6-bisphosp
hate aldolase (aldolase) to F- or G-actin provide first-encounter snapshots
of these interactions. Using x-ray structures of aldolase, G-actin, and th
ree-dimensional models of F-actin, the electrostatic potential about each p
rotein was predicted by solving the linearized Poisson-Boltzmann equation f
or use in BD simulations. The BD simulations provided solution complexes of
aldolase with F- or G-actin. All complexes demonstrate the close contacts
between oppositely charged regions of the protein surfaces. Positively char
ged surface regions of aldolase (residues Lys 13, 27, 288, 293, and 341 and
Arg 257) are attracted to the negatively charged amino terminus (Asp 1 and
Glu 2 and 4) and other patches (Asp 24, 25, and 363 and Glu 361, 364, 99,
and 100) of actin subunits. According to BD results, the most important fac
tor for aldolase binding to actin is the quaternary structure of aldolase a
nd actin. Two pairs of adjacent aldolase subunits greatly add to the positi
ve electrostatic potential of each other creating a region of attraction fo
r the negatively charged subdomain 1 of the actin subunit that is exposed t
o solvent in the quaternary F-actin structure.