The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins
| Autor: | X. Sharon Zhao, Andrew N. Amborski, Jamie J. Kwan, Logan W. Donaldson, Philip E. Johnson, Frank Sicheri, Tzvi Aviv |
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| Rok vydání: | 2005 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins biology Chemistry Saccharomyces cerevisiae Molecular Sequence Data RNA RNA-Binding Proteins RNA-binding protein Nuclear magnetic resonance spectroscopy Crystal structure biology.organism_classification Crystallography X-Ray Protein Structure Tertiary Crystallography Structural Biology Helix Domain (ring theory) Nucleic Acid Conformation Molecular Biology Sterile alpha motif Nuclear Magnetic Resonance Biomolecular |
| Zdroj: | Journal of molecular biology. 356(2) |
| ISSN: | 0022-2836 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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