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PMID: 16375924 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

The NMR and X-ray structures of the Saccharomyces cerevisiae Vts1 SAM domain define a surface for the recognition of RNA hairpins.

Journal of molecular biology ·Vol. 356 ·No. 2 ·2006-02-17 ·Pages 274-9

Aviv T, Amborski AN, Zhao XS, Kwan JJ, Johnson PE, Sicheri F, Donaldson LW

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.

MeSH Terms
Crystallography, X-Ray Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Nucleic Acid Conformation Protein Structure, Tertiary RNA/chemistry,metabolism RNA-Binding Proteins/chemistry,genetics,metabolism Saccharomyces cerevisiae Proteins/chemistry,genetics,metabolism
Chemicals
RNA-Binding Proteins Saccharomyces cerevisiae Proteins Vts1 protein, S cerevisiae RNA
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Aviv Tzvi
Program in Molecular Biology and Cancer, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ont., Canada.
Amborski Andrew N
Zhao X Sharon
Kwan Jamie J
Johnson Philip E
Sicheri Frank
Donaldson Logan W
Article Info
Journal
Journal of molecular biology
Abbr.
J Mol Biol
ISSN
0022-2836
Published
2006-02-17
Epub
2005-00-07
Pages
274-9
Language
English
Region
England
NLM ID
2985088R
Subset
IM
Databases
PDB
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