Structure determination at 2.4 angstrom resolution shows that lambda-e
xonuclease consists of three subunits that form a toroid. The central
channel is funnel shaped, tapering from an inner diameter of about 30
angstroms at the wider end to 15 angstroms at the narrow end. This is
adequate to accommodate the DNA substrate and thus provides a structur
al basis for the ability of the enzyme to sequentially hydrolyze thous
ands of nucleotides in a highly processive manner, The results also su
ggest the locations of the active sites and the constraints that limit
cleavage to a single strand.