1ng1
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N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
OverviewOverview
Ffh is a component of a bacterial ribonucleoprotein complex homologous to, the signal recognition particle (SRP) of eukaryotes. It comprises three, domains that mediate both binding to the hydrophobic signal sequence of, the nascent polypeptide and the GTP-dependent interaction of Ffh with a, structurally homologous GTPase of the SRP receptor. The X-ray structures, of the two-domain 'NG' GTPase of Ffh in complex with Mg2+GDP and GDP have, been determined at 2.0 A resolution. The structures explain the low, nucleotide affinity of Ffh and locate two regions of structural mobility, at opposite sides of the nucleotide-binding site. One of these regions, includes highly conserved sequence motifs that presumably contribute to, the structural trigger signaling the GTP-bound state. The other includes, the highly conserved interface between the N and G domains, and supports, the hypothesis that the N domain regulates or signals the nucleotide, occupancy of the G domain.
About this StructureAbout this Structure
1NG1 is a Single protein structure of sequence from Thermus aquaticus with , , , and as ligands. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
ReferenceReference
Functional changes in the structure of the SRP GTPase on binding GDP and Mg2+GDP., Freymann DM, Keenan RJ, Stroud RM, Walter P, Nat Struct Biol. 1999 Aug;6(8):793-801. PMID:10426959
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