Title of article :
The NMR and X-ray Structures of the Saccharomyces cerevisiae Vts1 SAM Domain Define a Surface for the Recognition of RNA Hairpins
Author/Authors :
Tzvi Aviv، نويسنده , , Andrew N. Amborski، نويسنده , , X. Sharon Zhao، نويسنده , , Jamie J. Kwan، نويسنده , , Philip E. Johnson، نويسنده , , Frank Sicheri، نويسنده , , Logan W. Donaldson، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2006
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 Å 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 α5 and the loop connecting helices α1 and α2.
Keywords :
NMR spectroscopy , X-ray crystallography , sterile alpha motif , translational repression
Journal title :
Journal of Molecular Biology
Journal title :
Journal of Molecular Biology