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2RP1

Refined solution structure of the PEMV-1 mRNA pseudoknot, regularized average structure

Summary for 2RP1
Entry DOI10.2210/pdb2rp1/pdb
Related1KPY 1KPZ 2RP0
DescriptorPEMV-1 mRNA pseudoknot (1 entity in total)
Functional Keywordsrna pseudoknot, frameshifting, rna
Total number of polymer chains1
Total formula weight8672.25
Authors
Cornish, P.V.,Hennig, M.,Giedroc, D.P. (deposition date: 2008-04-25, release date: 2009-03-31, Last modification date: 2024-05-29)
Primary citationGiedroc, D.P.,Cornish, P.V.
Frameshifting RNA pseudoknots: Structure and mechanism.
Virus Res., 139:193-208, 2009
Cited by
PubMed Abstract: Programmed ribosomal frameshifting (PRF) is one of the multiple translational recoding processes that fundamentally alters triplet decoding of the messenger RNA by the elongating ribosome. The ability of the ribosome to change translational reading frames in the -1 direction (-1 PRF) is employed by many positive strand RNA viruses, including economically important plant viruses and many human pathogens, such as retroviruses, e.g., HIV-1, and coronaviruses, e.g., the causative agent of severe acute respiratory syndrome (SARS), in order to properly express their genomes. -1 PRF is programmed by a bipartite signal embedded in the mRNA and includes a heptanucleotide "slip site" over which the paused ribosome "backs up" by one nucleotide, and a downstream stimulatory element, either an RNA pseudoknot or a very stable RNA stem-loop. These two elements are separated by six to eight nucleotides, a distance that places the 5' edge of the downstream stimulatory element in direct contact with the mRNA entry channel of the 30S ribosomal subunit. The precise mechanism by which the downstream RNA stimulates -1 PRF by the translocating ribosome remains unclear. This review summarizes the recent structural and biophysical studies of RNA pseudoknots and places this work in the context of our evolving mechanistic understanding of translation elongation. Support for the hypothesis that the downstream stimulatory element provides a kinetic barrier to the ribosome-mediated unfolding is discussed.
PubMed: 18621088
DOI: 10.1016/j.virusres.2008.06.008
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

226707

数据于2024-10-30公开中

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