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2A43

Crystal Structure of a Luteoviral RNA Pseudoknot and Model for a Minimal Ribosomal Frameshifting Motif

Summary for 2A43
Entry DOI10.2210/pdb2a43/pdb
DescriptorRNA Pseudoknot, MAGNESIUM ION (3 entities in total)
Functional Keywordsplrv, potato leaf roll virus; bwyv, beet western yellow virus, pk, pseudoknot, rna., rna
Total number of polymer chains1
Total formula weight8388.68
Authors
Pallan, P.S.,Marshall, W.S.,Harp, J.,Jewett III, F.C.,Wawrzak, Z.,Brown II, B.A.,Rich, A.,Egli, M. (deposition date: 2005-06-27, release date: 2005-09-27, Last modification date: 2023-08-23)
Primary citationPallan, P.S.,Marshall, W.S.,Harp, J.,Jewett III, F.C.,Wawrzak, Z.,Brown II, B.A.,Rich, A.,Egli, M.
Crystal Structure of a Luteoviral RNA Pseudoknot and Model for a Minimal Ribosomal Frameshifting Motif
Biochemistry, 44:11315-11322, 2005
Cited by
PubMed Abstract: To understand the role of structural elements of RNA pseudoknots in controlling the extent of -1-type ribosomal frameshifting, we determined the crystal structure of a high-efficiency frameshifting mutant of the pseudoknot from potato leaf roll virus (PLRV). Correlations of the structure with available in vitro frameshifting data for PLRV pseudoknot mutants implicate sequence and length of a stem-loop linker as modulators of frameshifting efficiency. Although the sequences and overall structures of the RNA pseudoknots from PLRV and beet western yellow virus (BWYV) are similar, nucleotide deletions in the linker and adjacent minor groove loop abolish frameshifting only with the latter. Conversely, mutant PLRV pseudoknots with up to four nucleotides deleted in this region exhibit nearly wild-type frameshifting efficiencies. The crystal structure helps rationalize the different tolerances for deletions in the PLRV and BWYV RNAs, and we have used it to build a three-dimensional model of the PRLV pseudoknot with a four-nucleotide deletion. The resulting structure defines a minimal RNA pseudoknot motif composed of 22 nucleotides capable of stimulating -1-type ribosomal frameshifts.
PubMed: 16114868
DOI: 10.1021/bi051061i
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.34 Å)
Structure validation

237735

数据于2025-06-18公开中

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