1C9S

CRYSTAL STRUCTURE OF A COMPLEX OF TRP RNA-BINDING ATTENUATION PROTEIN WITH A 53-BASE SINGLE STRANDED RNA CONTAINING ELEVEN GAG TRIPLETS SEPARATED BY AU DINUCLEOTIDES

1C9S の概要

• エントリーDOI: 10.2210/pdb1c9s/pdb
• NMR情報: BMRB: 5403
• 分子名称: SINGLE STRANDED RNA (55-MER), TRP RNA-BINDING ATTENUATION PROTEIN, TRYPTOPHAN, ... (4 entities in total)
• 機能のキーワード: trap, protein-rna complex, transcription, single stranded rna, rna binding protein-rna complex, rna binding protein/rna
• 由来する生物種: Geobacillus stearothermophilus; 詳細
• タンパク質・核酸の鎖数: 23
• 化学式量合計: 204519.38

構造登録者

Antson, A.A.,Dodson, E.J.,Dodson, G.G.,Greaves, R.B.,Chen, X.-P.,Gollnick, P. (登録日: 1999-08-03, 公開日: 1999-09-15, 最終更新日: 2024-02-07)

主引用文献

Antson, A.A.,Dodson, E.J.,Dodson, G.,Greaves, R.B.,Chen, X.,Gollnick, P.
Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA.
Nature, 401:235-242, 1999

PubMed Abstract: The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes of several bacilli by binding single-stranded RNA. The binding sequence is composed of eleven triplet repeats, predominantly GAG, separated by two or three non-conserved nucleotides. Here we present the crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets, revealing that each triplet is accommodated in a binding pocket formed by beta-strands. In the complex, the RNA has an extended structure without any base-pairing and binds to the protein mostly by specific protein-base interactions. Eleven binding pockets on the circular TRAP 11-mer form a belt with a diameter of about 80 A. This simple but elegant mechanism of arresting the RNA segment by encircling it around a protein disk is applicable to both transcription, when TRAP binds the nascent RNA, and to translation, when TRAP binds the same sequence within a non-coding leader region of the messenger RNA.

PubMed: 10499579
DOI: 10.1038/45730

実験手法

X-RAY DIFFRACTION (1.9 Å)