1FOW

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

Summary for 1FOW

• Entry DOI: 10.2210/pdb1fow/pdb
• Descriptor: L11-C76 (1 entity in total)
• Functional Keywords: ribosomal protein, rna-binding domain, l11-c76, alpha-helical protein, homeodomain fold
• Biological source: Geobacillus stearothermophilus
• Total number of polymer chains: 1
• Total formula weight: 8152.55

Authors

Markus, M.A.,Hinck, A.P.,Huang, S.,Draper, D.E.,Torchia, D.A. (deposition date: 1996-09-13, release date: 1997-03-12, Last modification date: 2024-05-22)

Primary citation

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

Experimental method

SOLUTION NMR