The crystal structure of T7 RNA polymerase reveals a molecule organize
d around a cleft that can accommodate a double-stranded DNA template.
A portion (approximately 45%) of the molecule displays extensive struc
tural homology to the polymerase domain of Klenow fragment and more li
mited homology to the human immunodeficiency virus HIV-1 reverse trans
criptase. A comparison of the structures and sequences of these polyme
rases identifies structural elements that may be responsible for discr
iminating between ribonucleotide and deoxyribonucleotide substrates, a
nd RNA and DNA templates. The relative locations of the catalytic site
and a specific promoter recognition residue allow the orientation of
the polymerase on the template to be defined.