1DUH

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

Summary for 1DUH

Entry DOI	10.2210/pdb1duh/pdb
Descriptor	4.5S RNA DOMAIN IV, LUTETIUM (III) ION, MAGNESIUM ION, ... (5 entities in total)
Functional Keywords	4.5s rna, domain iv, helix 8, signal recognition particle, srp, ffh, srp54, elongation factor g, ef-g, 23s rna, non-canonical base pairs, mismatch, rna
Total number of polymer chains	1
Total formula weight	15055.13
Authors	Jovine, L.,Hainzl, T.,Oubridge, C.,Scott, W.G.,Li, J.,Sixma, T.K.,Wonacott, A.,Skarzynski, T.,Nagai, K. (deposition date: 2000-01-17, release date: 2000-05-08, Last modification date: 2024-02-07)
Primary citation	Jovine, L.,Hainzl, T.,Oubridge, C.,Scott, W.G.,Li, J.,Sixma, T.K.,Wonacott, A.,Skarzynski, T.,Nagai, K. Crystal structure of the ffh and EF-G binding sites in the conserved domain IV of Escherichia coli 4.5S RNA. Structure Fold.Des., 8:527-540, 2000 Cited by PubMed 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. PubMed: 10801497 DOI: 10.1016/S0969-2126(00)00137-4 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.7 Å)

Structure validation