Structure of the conserved GTPase domain of the signal recognition particle.
Freymann, Douglas M.; Keenan, Robert J.; Stroud, Robert M.; Walter, Peter
[Letter] Nature. 385(6614):361-364, January 23, 1997.

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The signal-recognition particle (SRP) and its receptor (SR) function in the co-translational targeting of nascent protein-ribosome complexes to the membrane translocation apparatus [1]. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-alpha subunit (termed FtsY) [2,3]. Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other [4]. The sequence of Ffh suggests three domains: an amino-terminal N domain of unknown function, a central GTPase G domain, and a methionine-rich M domain that binds both SRP RNA and signal peptides [5,6]. Sequence conservation suggests that structurally similar N and G domains are present in FtsY [7,8]. Here we report the structure of the nucleotide-free form of the NG fragment of Ffh. Consistent with a role for apo Ffh in protein targeting, the side chains of the empty active-site pocket form a tight network of interactions which may stabilize the nucleotide-free protein. The structural relationship between the two domains suggests that the N domain senses or controls the nucleotide occupancy of the GTPase domain. A structural subdomain unique to these evolutionarily conserved GTPases constitutes them as a distinct subfamily in the GTPase superfamily [9].

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