1DUL

STRUCTURE OF THE RIBONUCLEOPROTEIN CORE OF THE E. COLI SIGNAL RECOGNITION PARTICLE

Summary for 1DUL

• Entry DOI: 10.2210/pdb1dul/pdb
• Descriptor: 4.5 S RNA DOMAIN IV, Signal recognition particle protein, POTASSIUM 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; More
• Total number of polymer chains: 2
• Total formula weight: 28843.96

Authors

Batey, R.T.,Rambo, R.P.,Lucast, L.,Rha, B.,Doudna, J.A. (deposition date: 2000-01-17, release date: 2000-02-28, Last modification date: 2020-10-14)

Primary citation

Batey, R.T.,Rambo, R.P.,Lucast, L.,Rha, B.,Doudna, J.A.
Crystal structure of the ribonucleoprotein core of the signal recognition particle.
Science, 287:1232-1239, 2000

PubMed Abstract: The signal recognition particle (SRP), a protein-RNA complex conserved in all three kingdoms of life, recognizes and transports specific proteins to cellular membranes for insertion or secretion. We describe here the 1.8 angstrom crystal structure of the universal core of the SRP, revealing protein recognition of a distorted RNA minor groove. Nucleotide analog interference mapping demonstrates the biological importance of observed interactions, and genetic results show that this core is functional in vivo. The structure explains why the conserved residues in the protein and RNA are required for SRP assembly and defines a signal sequence recognition surface composed of both protein and RNA.

PubMed: 10678824
DOI: 10.1126/science.287.5456.1232

Experimental method

X-RAY DIFFRACTION (1.8 Å)