Structure of the conserved GTPase domain of the signal recognition particle

Douglas M. Freymann*, Robert J. Keenan, Robert M. Stroud, Peter Walter

*Corresponding author for this work

Research output: Contribution to journalArticle

189 Scopus citations

Abstract

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. The SRP protein subunit (termed Ffh in bacteria) that recognizes the signal sequence of nascent polypeptides is a GTPase, as is the SR-α subunit (termed FtsY). Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other. The sequence of Fin 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. Sequence conservation suggests that structurally similar N and G domains are present in FtsY. 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.

Original languageEnglish (US)
Pages (from-to)361-364
Number of pages4
JournalNature
Volume385
Issue number6614
DOIs
StatePublished - Jan 23 1997

ASJC Scopus subject areas

  • General

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