Newly synthesized proteins destined either for secretion or incorporat
ion into membranes are targeted to the membrane translocation machiner
y by a ubiquitous system consisting of a signal recognition particle (
SRP) and its receptor(1,2). Both the SRP receptor and the protein with
in the SRP that binds the signal sequence contain GTPases(3,4). These
two proteins, together with the RNA component of the SRP, form a compl
ex(5-7) and thereby regulate each other's GTPase activity(8). Here we
report the structure of the GTPase-containing portion of FtsY, the fun
ctional homologue of the SRP receptor of Escherichia coli(9), at 2.2 A
ngstrom resolution without bound nucleotide. This so-called NG domain
displays similarities to the Ras-related GTPases, as well as features
unique to the SRP-type GTPases(10), such as a separate aminoterminal d
omain, an insertion within the p21(ras) (Ras) effector domain(11), and
a wide-open GTP-binding region. The structure explains the low affini
ty of FtsY for GTP, and suggests rearrangements that may occur on nucl
eotide binding. It also identifies regions potentially involved in the
transmission of signals between domains and in interactions with regu
latory proteins.