PMID:10801497

Citation	Jovine, L, Hainzl, T, Oubridge, C, Scott, WG, Li, J, Sixma, TK, Wonacott, A, Skarzynski, T and Nagai, K (2000) Crystal structure of the ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA. Structure 8:527-40
Abstract	Bacterial signal recognition particle (SRP), consisting of 4.5S RNA and Ffh protein, plays an essential role in targeting signal-peptide-containing proteins to the secretory apparatus in the cell membrane. The 4.5S RNA increases the affinity of Ffh for signal peptides and is essential for the interaction between SRP and its receptor, protein FtsY. The 4.5S RNA also interacts with elongation factor G (EF-G) in the ribosome and this interaction is required for efficient translation.
Links	PubMed
Keywords	Bacterial Proteins/metabolism; Base Pairing; Base Sequence; Binding Sites/genetics; Conserved Sequence; Crystallography, X-Ray; Dimerization; Escherichia coli/genetics; Escherichia coli Proteins; Guanine Nucleotides/chemistry; Lutetium/chemistry; Models, Molecular; Molecular Sequence Data; Peptide Elongation Factor G/metabolism; Protein Structure, Tertiary; RNA, Bacterial; RNA, Ribosomal/chemistry; RNA, Ribosomal/metabolism; Signal Recognition Particle/metabolism
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