1A4T

SOLUTION STRUCTURE OF PHAGE P22 N PEPTIDE-BOX B RNA COMPLEX, NMR, 20 STRUCTURES

1A4T の概要

• エントリーDOI: 10.2210/pdb1a4t/pdb
• 分子名称: BOXB RNA, 20-MER BASIC PEPTIDE (2 entities in total)
• 機能のキーワード: bacteriophage transcriptional antitermination, peptide-rna recognition, gnra loop, bent alpha-helical peptide, transcription regulation, transcription-rna complex, transcription/rna
• 由来する生物種: Enterobacteria phage P22
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 7245.75

構造登録者

Cai, Z.,Gorin, A.A.,Frederick, R.,Ye, X.,Hu, W.,Majumdar, A.,Kettani, A.,Patel, D.J. (登録日: 1998-02-04, 公開日: 1998-04-29, 最終更新日: 2024-05-22)

主引用文献

Cai, Z.,Gorin, A.,Frederick, R.,Ye, X.,Hu, W.,Majumdar, A.,Kettani, A.,Patel, D.J.
Solution structure of P22 transcriptional antitermination N peptide-boxB RNA complex.
Nat.Struct.Biol., 5:203-212, 1998

PubMed Abstract: We have determined the solution structure of a 15-mer boxB RNA hairpin complexed with a 20-mer basic peptide of the N protein involved in bacteriophage P22 transcriptional antitermination. Complex formation involves adaptive binding with the N peptide adopting a bent alpha-helical conformation that packs tightly through hydrophobic and electrostatic interactions against the major groove face of the boxB RNA hairpin, orienting the open opposite face for potential interactions with host factors and/or RNA polymerase. Four nucleotides in the boxB RNA hairpin pentaloop form a stable GNRA like tetraloop structural scaffold on complex formation, allowing the looped out fifth nucleotide to make extensive hydrophobic contacts with the bound peptide. The guanidinium group of a key arginine is hydrogen-bonded to the guanine in a loop-closing sheared G.A mismatch and to adjacent backbone phosphates. The identified intermolecular contacts account for the consequences of N peptide and boxB RNA mutations on bacteriophage transcriptional antitermination.

PubMed: 9501914
DOI: 10.1038/nsb0398-203

実験手法

SOLUTION NMR