The conformational changes that the GroEL oligomer undergoes upon nucleotide and cochaperonin GroES binding have been studied using electron microscopy and image processing techniques. Average side views of the three allosteric states (TT, TR, and RR, which correspond to none, one, or both of the two heptameric rings of the GroEL oligomer occupied by nucleotide, respectively) of GroEL and GroEL-GroES complexes for ADP, ATP, and two nonhydrolyzable analogs (AMP-PNP and ATP gamma S) have been obtained at 20-25 A resolution. Both AMP-PNP and ATP induce similar conformational shifts in the apical domains of GroEL. At the TR state, only one of the GroEL rings shows an upward and outward movement of the apical domains ("open state"). At the RR state for AMP-PNP and ATP, both GroEL rings undergo conformational changes, albeit of different magnitude, giving rise to a structurally asymmetric particle (one ring in the "open" state, while the other is in an "intermediate" state). These changes are also observed when GroEL is incubated with ADP and Pi, but not with ADP, which suggests that upon ATP binding, GroEL undergoes a conformational change that is partly maintained after ATP hydrolysis and as long as ADP and Pi are bound to the GroEL ring. The conformational changes undergone by GroEL are discussed within the framework of a proposed GroEL cycle mechanism.