2f8k | pdb_00002f8k
Sequence specific recognition of RNA hairpins by the SAM domain of Vts1
Structural highlights
FunctionVTS1_YEAST RNA-binding protein involved in post-transcriptional regulation through transcript degradation of SRE (SMG-recognition elements) bearing mRNAs. May be involved in vacuolar protein transport.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe SAM domain of the Saccharomyces cerevisiae post-transcriptional regulator Vts1p epitomizes a subfamily of SAM domains conserved from yeast to humans that function as sequence-specific RNA-binding domains. Here we report the 2.0-A X-ray structure of the Vts1p SAM domain bound to a high-affinity RNA ligand. Specificity of RNA binding arises from the association of a guanosine loop base with a shallow pocket on the SAM domain and from multiple SAM domain contacts to the unique backbone structure of the loop, defined in part by a nonplanar base pair within the loop. We have validated NNF1 as an endogenous target of Vts1p among 79 transcripts that copurify with Vts1p. Bioinformatic analysis of these mRNAs demonstrates that the RNA-binding specificity of Vts1p in vivo is probably more stringent than that of the isolated SAM domain in vitro. Sequence-specific recognition of RNA hairpins by the SAM domain of Vts1p.,Aviv T, Lin Z, Ben-Ari G, Smibert CA, Sicheri F Nat Struct Mol Biol. 2006 Feb;13(2):168-76. Epub 2006 Jan 22. PMID:16429151[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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