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PDBsum entry 2f8k

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RNA binding protein/ RNA PDB id
2f8k
Contents
Protein chain
84 a.a.
DNA/RNA
Waters ×117

References listed in PDB file
Key reference
Title Sequence-Specific recognition of RNA hairpins by the sam domain of vts1p.
Authors T.Aviv, Z.Lin, G.Ben-Ari, C.A.Smibert, F.Sicheri.
Ref. Nat Struct Mol Biol, 2006, 13, 168-176. [DOI no: 10.1038/nsmb1053]
PubMed id 16429151
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 0%.
Abstract
The 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.
Figure 2.
Figure 2. The SRE pentaloop structure exhibits similarity to the UNCG and SECIS loops. (a) Stereo diagram of the SRE pentaloop. Dashed lines indicate hydrogen bonds. (b,c) Stereo diagrams of the SRE crystal structure overlaid with the UNCG (b, green; PDB entry 1F7Y; ref. 21) and SECIS (c, blue; PDB entry 1WSU; ref. 22) RNA loops, respectively. Superpositions were generated with Swiss-PDB viewer (http://www.expasy.org/spdbv/).
Figure 3.
Figure 3. Features of the Vts1p-SAM–RNA binding interface. (a) Schematic diagram of SRE recognition by Vts1p-SAM. Black dashed lines, hydrogen bonds; green dashed lines, hydrophobic interactions; blue background, the stem of the SRE; pink background, the pentaloop; red circles, phosphate groups; blue ovals, bridging water molecules. The labeled protein residues are colored according to their originating secondary structure elements as shown in the upper left schematic. (b) Stereo diagram of the Vts1p-SAM–SRE binding interface centered on SRE loop position G3. Red spheres, water molecules participating in bridging interactions between protein and RNA; dashed lines, hydrogen bonds involving the G3 base.
The above figures are reprinted by permission from Macmillan Publishers Ltd: Nat Struct Mol Biol (2006, 13, 168-176) copyright 2006.
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