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2O33

Solution structure of U2 snRNA stem I from S. cerevisiae

Summary for 2O33
Entry DOI10.2210/pdb2o33/pdb
Related2O32
NMR InformationBMRB: 15080,15081
DescriptorU2 snRNA (1 entity in total)
Functional Keywordsrna, wobble base-pairs, u2 snrna, ribonucleic acid
Total number of polymer chains1
Total formula weight6291.68
Authors
Sashital, D.G.,Venditti, V.,Angers, C.A.,Cornilescu, G.,Butcher, S.E. (deposition date: 2006-11-30, release date: 2007-02-06, Last modification date: 2023-12-27)
Primary citationSashital, D.G.,Venditti, V.,Angers, C.G.,Cornilescu, G.,Butcher, S.E.
Structure and thermodynamics of a conserved U2 snRNA domain from yeast and human.
Rna, 13:328-338, 2007
Cited by
PubMed Abstract: The spliceosome is a dynamic ribonucleoprotein complex responsible for the removal of intron sequences from pre-messenger RNA. The highly conserved 5' end of the U2 small nuclear RNA (snRNA) makes key base-pairing interactions with the intron branch point sequence and U6 snRNA. U2 stem I, a stem-loop located in the 5' region of U2, has been implicated in spliceosome assembly and may modulate the folding of the U2 and U6 snRNAs in the spliceosome active site. Here we present the NMR structures of U2 stem I from human and Saccharomyces cerevisiae. These sequences represent the two major classes of U2 stem I, distinguished by the identity of tandem wobble pairs (UU/UU in yeast and CA/GU in human) and the presence of post-transcriptional modifications (four 2'-O-methyl groups and two pseudouracils in human). The structures reveal that the UU/UU and CA/GU tandem wobble pairs are nearly isosteric. The tandem wobble pairs separate two thermodynamically distinct regions of Watson-Crick base pairs, with the modified nucleotides in human stem I conferring a significant increase in stability. We hypothesize that the separate thermodynamic stabilities of U2 stem I exist to allow the structure to transition through different folded conformations during spliceosome assembly and catalysis.
PubMed: 17242306
DOI: 10.1261/rna.418407
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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数据于2024-10-30公开中

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