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N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
Overview
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 ... [(full description)]
About this Structure
1FFH is a [Single protein] structure of sequence from [Thermus aquaticus] with MG as [ligand]. Structure known Active Sites: I, II, III and IV. Full crystallographic information is available from [OCA].
Reference
Structure of the conserved GTPase domain of the signal recognition particle., Freymann DM, Keenan RJ, Stroud RM, Walter P, Nature. 1997 Jan 23;385(6614):361-4. PMID:9002524
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