1duh

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spinqualitylabelsall models 1duh, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF THE CONSERVED DOMAIN IV OF E. COLI 4.5S RNA

Overview

BACKGROUND: 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., RESULTS: We have determined by multiple anomalous dispersion (MAD) with, Lu(3+) the 2.7 A crystal structure of a 4.5S RNA fragment containing, binding sites for both Ffh and EF-G. This fragment consists of three, helices connected by a symmetric and an asymmetric internal loop. In, contrast to NMR-derived structures reported previously, the symmetric loop, is entirely constituted by non-canonical base pairs. These pairs, continuously stack and project unusual sets of hydrogen-bond donors and, acceptors into the shallow minor groove. The structure can therefore be, regarded as two double helical rods hinged by the asymmetric loop that, protrudes from one strand. CONCLUSIONS: Based on our crystal structure and, results of chemical protection experiments reported previously, we, predicted that Ffh binds to the minor groove of the symmetric loop. An, identical decanucleotide sequence is found in the EF-G binding sites of, both 4.5S RNA and 23S rRNA. The decanucleotide structure in the 4.5S RNA, and the ribosomal protein L11-RNA complex crystals suggests how 4.5S RNA, and 23S rRNA might interact with EF-G and function in translating, ribosomes.

About this Structure

1DUH is a Single protein structure of sequence from [1] with LU, MG and SO4 as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA., Jovine L, Hainzl T, Oubridge C, Scott WG, Li J, Sixma TK, Wonacott A, Skarzynski T, Nagai K, Structure. 2000 May 15;8(5):527-40. PMID:10801497

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