2FE9

Solution structure of the Vts1 SAM domain in the presence of RNA

2FE9 の概要

• エントリーDOI: 10.2210/pdb2fe9/pdb
• NMR情報: BMRB: 6922
• 分子名称: Protein VTS1 (1 entity in total)
• 機能のキーワード: vts1, sam domain, smaug, rna binding protein, translational control
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9879.55

構造登録者

Edwards, T.A.,Butterwick, J.A.,Palmer, A.G.,Aggarwal, A.K. (登録日: 2005-12-15, 公開日: 2006-01-24, 最終更新日: 2024-05-08)

主引用文献

Edwards, T.A.,Butterwick, J.A.,Zeng, L.,Gupta, Y.K.,Wang, X.,Wharton, R.P.,Palmer, A.G.,Aggarwal, A.K.
Solution Structure of the Vts1 SAM Domain in the Presence of RNA.
J.Mol.Biol., 356:1065-1072, 2006

PubMed Abstract: The yeast Vts1 SAM (sterile alpha motif) domain is a member of a new class of SAM domains that specifically bind RNA. To elucidate the structural basis for RNA binding, the solution structure of the Vts1 SAM domain, in the presence of a specific target RNA, has been solved by multidimensional heteronuclear NMR spectroscopy. The Vts1 SAM domain retains the "core" five-helix-bundle architecture of traditional SAM domains, but has additional short helices at N and C termini, comprising a small substructure that caps the core helices. The RNA-binding surface of Vts1, determined by chemical shift perturbation, maps near the ends of three of the core helices, in agreement with mutational data and the electrostatic properties of the molecule. These results provide a structural basis for the versatility of the SAM domain in protein and RNA-recognition.

PubMed: 16405996
DOI: 10.1016/j.jmb.2005.12.004

実験手法

SOLUTION NMR