Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2190145 | Journal of Molecular Biology | 2006 | 6 Pages |
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.
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Authors
Tzvi Aviv, Andrew N. Amborski, X. Sharon Zhao, Jamie J. Kwan, Philip E. Johnson, Frank Sicheri, Logan W. Donaldson,