2D3D
crystal structure of the RNA binding SAM domain of saccharomyces cerevisiae Vts1
Summary for 2D3D
Entry DOI | 10.2210/pdb2d3d/pdb |
Descriptor | Vts1 protein, CALCIUM ION (3 entities in total) |
Functional Keywords | rna binding, sam domain, sre hairpin binding, rna binding protein |
Biological source | Saccharomyces cerevisiae (baker's yeast) |
Total number of polymer chains | 1 |
Total formula weight | 10119.86 |
Authors | Aviv, T.,Amborski, A.N.,Zhao, X.S.,Kwan, J.J.,Johnson, P.E.,Sicheri, F.,Donaldson, L.W. (deposition date: 2005-09-27, release date: 2006-02-14, Last modification date: 2024-03-13) |
Primary citation | Aviv, T.,Amborski, A.N.,Zhao, X.S.,Kwan, J.J.,Johnson, P.E.,Sicheri, F.,Donaldson, L.W. The NMR and X-ray Structures of the Saccharomyces cerevisiae Vts1 SAM Domain Define a Surface for the Recognition of RNA Hairpins J.Mol.Biol., 356:274-279, 2006 Cited by PubMed Abstract: The SAM domain of the Saccharomyces cerevisiae post-transcriptional regulator Vts1 has a high affinity towards RNA hairpins containing a CUGGC pentaloop. We present the 1.6 Angstroms X-ray crystal structure of the Vts1 SAM domain in its unliganded state, and the NMR solution structure of this domain in its RNA-bound state. Both structures reveal a canonical five helix SAM domain flanked by additional secondary structural elements at the N and C termini. The two structures are essentially identical, implying that no major structural rearrangements occur upon RNA binding. Amide chemical shift changes map the RNA-binding site to a shallow, basic patch at the junction of helix alpha5 and the loop connecting helices alpha1 and alpha2. PubMed: 16375924DOI: 10.1016/j.jmb.2005.11.066 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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