1HQ1

STRUCTURAL AND ENERGETIC ANALYSIS OF RNA RECOGNITION BY A UNIVERSALLY CONSERVED PROTEIN FROM THE SIGNAL RECOGNITION PARTICLE

1HQ1 の概要

• エントリーDOI: 10.2210/pdb1hq1/pdb
• 分子名称: 4.5S RNA DOMAIN IV, SIGNAL RECOGNITION PARTICLE PROTEIN, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: protein-rna complex, double helix, tetraloop, internal loop, signal recognition particle, srp, ribonucleoprotein, signaling protein-rna complex, signaling protein/rna
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 28187.43

構造登録者

Batey, R.T.,Sagar, M.B.,Doudna, J.A. (登録日: 2000-12-13, 公開日: 2001-01-03, 最終更新日: 2023-08-09)

主引用文献

Batey, R.T.,Sagar, M.B.,Doudna, J.A.
Structural and energetic analysis of RNA recognition by a universally conserved protein from the signal recognition particle.
J.Mol.Biol., 307:229-246, 2001

PubMed Abstract: The signal recognition particle (SRP) is a ribonucleoprotein complex responsible for targeting proteins to the endoplasmic reticulum in eukarya or to the inner membrane in prokarya. The crystal structure of the universally conserved RNA-protein core of the Escherichia coli SRP, refined here to 1.5 A resolution, revealed minor groove recognition of the 4.5 S RNA component by the M domain of the Ffh protein. Within the RNA, nucleotides comprising two phylogenetically conserved internal loops create a unique surface for protein recognition. To determine the energetic importance of conserved nucleotides for SRP assembly, we measured the affinity of the M domain for a series of RNA mutants. This analysis reveals how conserved nucleotides within the two internal loop motifs establish the architecture of the macromolecular interface and position essential functional groups for direct recognition by the protein.

PubMed: 11243816
DOI: 10.1006/jmbi.2000.4454

実験手法

X-RAY DIFFRACTION (1.52 Å)