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(2): 274-9, 2006 Feb 17.
Article
em En
| MEDLINE
| ID: mdl-16375924
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.
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Base de dados:
MEDLINE
Assunto principal:
RNA
/
Proteínas de Ligação a RNA
/
Estrutura Terciária de Proteína
/
Proteínas de Saccharomyces cerevisiae
/
Conformação de Ácido Nucleico
Idioma:
En
Revista:
J Mol Biol
Ano de publicação:
2006
Tipo de documento:
Article
País de afiliação:
Canadá