2ESE

Structure of the SAM domain of Vts1p in complex with RNA

Summary for 2ESE

• Entry DOI: 10.2210/pdb2ese/pdb
• Descriptor: 5'-R(*GP*GP*AP*GP*AP*GP*GP*CP*UP*CP*UP*GP*GP*CP*AP*GP*CP*UP*UP*UP*UP*CP*C)-3', Vts1p (2 entities in total)
• Functional Keywords: protein-rna complex, shape specific recognition, sam domain, stem-loop, protein-rna complex complex, protein/rna complex
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Total number of polymer chains: 2
• Total formula weight: 18933.87

Authors

Allain, F.H.T. (deposition date: 2005-10-26, release date: 2006-01-24, Last modification date: 2024-05-22)

Primary citation

Oberstrass, F.C.,Lee, A.,Stefl, R.,Janis, M.,Chanfreau, G.,Allain, F.H.
Shape-specific recognition in the structure of the Vts1p SAM domain with RNA.
Nat.Struct.Mol.Biol., 13:160-167, 2006

PubMed Abstract: Although the abundant sterile alpha motif (SAM) domain was originally classified as a protein-protein interaction domain, it has recently been shown that certain SAM domains have the ability to bind RNA, defining a new type of post-transcriptional gene regulator. To further understand the function of SAM-RNA recognition, we determined the solution structures of the SAM domain of the Saccharomyces cerevisiae Vts1p (Vts1p-SAM) and the Smaug response element (SRE) stem-loop RNA as a complex and in isolation. The structures show that Vts1p-SAM recognizes predominantly the shape of the SRE rather than its sequence, with the exception of a G located at the tip of the pentaloop. Using microarray gene profiling, we identified several genes in S. cerevisiae that seem to be regulated by Vts1p and contain one or more copies of the SRE.

PubMed: 16429156
DOI: 10.1038/nsmb1038

Experimental method

SOLUTION NMR