1ACI

L11 RIBOSOMAL PROTEIN RNA BINDING DOMAIN, NMR, 20 STRUCTURES

1ACI の概要

• エントリーDOI: 10.2210/pdb1aci/pdb
• 分子名称: L11 RIBOSOMAL PROTEIN (1 entity in total)
• 機能のキーワード: l11-c76, ribosomal protein
• 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

Xing, Y.,Draper, D.E. (登録日: 1997-02-07, 公開日: 1998-01-14, 最終更新日: 2024-05-22)

主引用文献

Xing, Y.,Draper, D.E.
Cooperative interactions of RNA and thiostrepton antibiotic with two domains of ribosomal protein L11.
Biochemistry, 35:1581-1588, 1996

PubMed Abstract: Ribosomal protein L11 interacts with a 58-nucleotide domain of large subunit ribosomal RNA; both the protein and its RNA target have been highly conserved. The antibiotic thiostrepton recognizes the same RNA domain, and binds to the ribosome cooperatively with L11. Experiments presented here show that RNA recognition and thiostrepton cooperativity can be attributed to C- and N-terminal domains of L11, respectively. Under trypsin digestion conditions that degrade Bacillus stearothermophilus L11 to small fragments, the target RNA protects the C-terminal 77 residues from digestion, and thiostrepton and RNA in combination protect the entire protein. A 76-residue C-terminal fragment of L11 was overexpressed and shown to fold into a stable structure binding ribosomal RNA with essentially the same properties as full-length L11. An L11.thiostrepton.RNA complex was 100-200-fold more stable than expected on the basis of L11-RNA and thiostrepton-RNA binding affinities; similar measurements with the C-terminal fragment detected no cooperativity with thiostrepton. L11 function is thus more complex than simple interaction with ribosomal RNA; we suggest that thiostrepton mimics some ribosomal component or factor that normally interacts with the L11 N-terminal domain.

PubMed: 8634289
DOI: 10.1021/bi952132o

実験手法

SOLUTION NMR