1FOW

NMR STRUCTURE OF L11-C76, THE C-TERMINAL DOMAIN OF 50S RIBOSOMAL PROTEIN L11, MINIMIZED AVERAGE STRUCTURE

1FOW の概要

• エントリーDOI: 10.2210/pdb1fow/pdb
• 分子名称: L11-C76 (1 entity in total)
• 機能のキーワード: ribosomal protein, rna-binding domain, l11-c76, alpha-helical protein, homeodomain fold
• 由来する生物種: Geobacillus stearothermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 8152.55

構造登録者

Markus, M.A.,Hinck, A.P.,Huang, S.,Draper, D.E.,Torchia, D.A. (登録日: 1996-09-13, 公開日: 1997-03-12, 最終更新日: 2024-05-22)

主引用文献

Markus, M.A.,Hinck, A.P.,Huang, S.,Draper, D.E.,Torchia, D.A.
High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA.
Nat.Struct.Biol., 4:70-77, 1997

PubMed Abstract: The structure of the C-terminal RNA recognition domain of ribosomal protein L11 has been solved by heteronuclear three-dimensional nuclear magnetic resonance spectroscopy. Although the structure can be considered high resolution in the core, 15 residues between helix alpha 1 and strand beta 1 form an extended, unstructured loop. 15N transverse relaxation measurements suggest that the loop is moving on a picosecond-to-nanosecond time scale in the free protein but not in the protein bound to RNA. Chemical shifts differences between the free protein and the bound protein suggest that the loop as well as the C-terminal end of helix alpha 3 are involved in RNA binding.

PubMed: 8989327
DOI: 10.1038/nsb0197-70

実験手法

SOLUTION NMR