2B6G
RNA recognition by the Vts1 SAM domain
Summary for 2B6G
Entry DOI | 10.2210/pdb2b6g/pdb |
Related | 2D3D |
NMR Information | BMRB: 6956 |
Descriptor | 5'-R(*GP*GP*AP*GP*GP*CP*UP*CP*UP*GP*GP*CP*AP*GP*CP*UP*UP*UP*C)-3', Vts1p (2 entities in total) |
Functional Keywords | alpha-helix, pentaloop, hairpin, rna binding protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) More |
Total number of polymer chains | 2 |
Total formula weight | 19183.49 |
Authors | Donaldson, L.W.,Johnson, P.E. (deposition date: 2005-10-01, release date: 2006-01-24, Last modification date: 2024-05-22) |
Primary citation | Johnson, P.E.,Donaldson, L.W. RNA recognition by the Vts1p SAM domain Nat.Struct.Mol.Biol., 13:177-178, 2006 Cited by PubMed Abstract: The putative yeast post-transcriptional regulator Vts1p and its related protein Smaug, from Drosophila melanogaster, each use a sterile alpha motif (SAM) domain to bind an RNA hairpin termed the Smaug recognition element (SRE). Here, we present the NMR structures of the Vts1p-SRE complex and the free SRE. Structural highlights include the direct recognition of a guanine base and the formation or stabilization of a base pair in the SRE loop. PubMed: 16429155DOI: 10.1038/nsmb1039 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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