1HQ1

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

Summary for 1HQ1

• Entry DOI: 10.2210/pdb1hq1/pdb
• Descriptor: 4.5S RNA DOMAIN IV, SIGNAL RECOGNITION PARTICLE PROTEIN, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: protein-rna complex, double helix, tetraloop, internal loop, signal recognition particle, srp, ribonucleoprotein, signaling protein-rna complex, signaling protein/rna
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 28187.43

Authors

Batey, R.T.,Sagar, M.B.,Doudna, J.A. (deposition date: 2000-12-13, release date: 2001-01-03, Last modification date: 2023-08-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.52 Å)