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http://purl.uniprot.org/citations/9002524http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9002524http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9002524http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9002524http://www.w3.org/2000/01/rdf-schema#comment"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-alpha subunit (termed FtsY). Ffh and FtsY interact directly, each stimulating the GTP hydrolysis activity of the other. 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. 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."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.org/dc/terms/identifier"doi:10.1038/385361a0"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.org/dc/terms/identifier"doi:10.1038/385361a0"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Stroud R.M."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Stroud R.M."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Walter P."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Walter P."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Keenan R.J."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Keenan R.J."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Freymann D.M."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/author"Freymann D.M."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/date"1997"xsd:gYear
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/pages"361-364"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/pages"361-364"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/title"Structure of the conserved GTPase domain of the signal recognition particle."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/title"Structure of the conserved GTPase domain of the signal recognition particle."xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/volume"385"xsd:string
http://purl.uniprot.org/citations/9002524http://purl.uniprot.org/core/volume"385"xsd:string
http://purl.uniprot.org/citations/9002524http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9002524