2FE9
Solution structure of the Vts1 SAM domain in the presence of RNA
Summary for 2FE9
| Entry DOI | 10.2210/pdb2fe9/pdb |
| NMR Information | BMRB: 6922 |
| Descriptor | Protein VTS1 (1 entity in total) |
| Functional Keywords | vts1, sam domain, smaug, rna binding protein, translational control |
| Biological source | Saccharomyces cerevisiae (baker's yeast) |
| Total number of polymer chains | 1 |
| Total formula weight | 9879.55 |
| Authors | Edwards, T.A.,Butterwick, J.A.,Palmer, A.G.,Aggarwal, A.K. (deposition date: 2005-12-15, release date: 2006-01-24, Last modification date: 2024-05-08) |
| Primary citation | Edwards, T.A.,Butterwick, J.A.,Zeng, L.,Gupta, Y.K.,Wang, X.,Wharton, R.P.,Palmer, A.G.,Aggarwal, A.K. Solution Structure of the Vts1 SAM Domain in the Presence of RNA. J.Mol.Biol., 356:1065-1072, 2006 Cited by PubMed Abstract: The yeast Vts1 SAM (sterile alpha motif) domain is a member of a new class of SAM domains that specifically bind RNA. To elucidate the structural basis for RNA binding, the solution structure of the Vts1 SAM domain, in the presence of a specific target RNA, has been solved by multidimensional heteronuclear NMR spectroscopy. The Vts1 SAM domain retains the "core" five-helix-bundle architecture of traditional SAM domains, but has additional short helices at N and C termini, comprising a small substructure that caps the core helices. The RNA-binding surface of Vts1, determined by chemical shift perturbation, maps near the ends of three of the core helices, in agreement with mutational data and the electrostatic properties of the molecule. These results provide a structural basis for the versatility of the SAM domain in protein and RNA-recognition. PubMed: 16405996DOI: 10.1016/j.jmb.2005.12.004 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
