In this figure, one monomer of 14-3-3 is shown bound to the acetyltransferase enzyme. The scattered dots represent the portion of the molecular surface of 14-3-3 that interacts with the acetyltransferase.
Interestingly, most of the interaction surface is distant from the site of phosphorylation on the N-terminal tail of the enzyme. Indeed, a large part of the interaction involves those regions of the enzyme that rearrange during its catalytic cycle (which is shown here ). It appears that 14-3-3 stabilizes the conformation of the enzyme in which the substrates are bound. The conformation of the free enzyme (i.e., without substrates) is not compatible with this complex.