430D
STRUCTURE OF SARCIN/RICIN LOOP FROM RAT 28S RRNA
Summary for 430D
Entry DOI | 10.2210/pdb430d/pdb |
Descriptor | SARCIN/RICIN LOOP FROM RAT 28S R-RNA, MAGNESIUM ION (3 entities in total) |
Functional Keywords | u-rna, double helix, hairpin, blunt stem, tetraloop mismatched, base triple, ribonucleic acid, rna |
Biological source | Rattus norvegicus |
Total number of polymer chains | 1 |
Total formula weight | 9674.32 |
Authors | Correll, C.C.,Munishkin, A.,Chan, Y.L.,Ren, Z.,Wool, I.G.,Steitz, T.A. (deposition date: 1998-10-04, release date: 1998-10-07, Last modification date: 2024-02-28) |
Primary citation | Correll, C.C.,Munishkin, A.,Chan, Y.L.,Ren, Z.,Wool, I.G.,Steitz, T.A. Crystal structure of the ribosomal RNA domain essential for binding elongation factors. Proc.Natl.Acad.Sci.USA, 95:13436-13441, 1998 Cited by PubMed Abstract: The structure of a 29-nucleotide RNA containing the sarcin/ricin loop (SRL) of rat 28 S rRNA has been determined at 2.1 A resolution. Recognition of the SRL by elongation factors and by the ribotoxins, sarcin and ricin, requires a nearly universal dodecamer sequence that folds into a G-bulged cross-strand A stack and a GAGA tetraloop. The juxtaposition of these two motifs forms a distorted hairpin structure that allows direct recognition of bases in both grooves as well as recognition of nonhelical backbone geometry and two 5'-unstacked purines. Comparisons with other RNA crystal structures establish the cross-strand A stack and the GNRA tetraloop as defined and modular RNA structural elements. The conserved region at the top is connected to the base of the domain by a region presumed to be flexible because of the sparsity of stabilizing contacts. Although the conformation of the SRL RNA previously determined by NMR spectroscopy is similar to the structure determined by x-ray crystallography, significant differences are observed in the "flexible" region and to a lesser extent in the G-bulged cross-strand A stack. PubMed: 9811818DOI: 10.1073/pnas.95.23.13436 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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