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1DUL

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

Summary for 1DUL
Entry DOI10.2210/pdb1dul/pdb
Descriptor4.5 S RNA DOMAIN IV, Signal recognition particle protein, POTASSIUM ION, ... (5 entities in total)
Functional Keywordsprotein-rna complex, double helix, tetraloop, internal loop, signal recognition particle, srp, ribonucleoprotein, signaling protein-rna complex, signaling protein/rna
Biological sourceEscherichia coli
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Total number of polymer chains2
Total formula weight28843.96
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: 2024-11-20)
Primary citationBatey, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

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