Crystal structure of the NG domain from the signal-recognition particle receptor FtsY

Guillermo Montoya, Cecilia Svensson, Joen Luirink and Irmgard Sinning
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Guillermo Montoya: Structural Biology Programme
Cecilia Svensson: Structural Biology Programme
Joen Luirink: Structural Biology Programme
Irmgard Sinning: Structural Biology Programme

Nature, 1997, vol. 385, issue 6614, 365-368

Abstract: Abstract Newly synthesized proteins destined either for secretion or incorporation into membranes are targeted to the membrane translocation machinery by a ubiquitous system consisting of a signal-recognition particle (SRP) and its receptor1,2. Both the SRP receptor and the protein within the SRP that binds the signal sequence contain GTPases3,4. These two proteins, together with the RNA component of the SRP, form a complex5–7 and thereby regulate each other's GTPase activity8. Here we report the structure of the GTPase-containing portion of FtsY, the functional homologue of the SRP receptor of Escherichia coli9, at 2.2 Å 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 GTPases10, such as a separate amino-terminal domain, an insertion within the p21ras (Ras) effector domain11, and a wide-open GTP-binding region. The structure explains the low affinity of FtsY for GTP, and suggests rearrangements that may occur on nucleotide binding. It also identifies regions potentially involved in the transmission of signals between domains and in interactions with regulatory proteins.

Date: 1997
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DOI: 10.1038/385365a0

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