1dul | pdb_00001dul

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

File:1dul.jpg


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1dul, resolution 1.80Å
Ligands: A, C, CCC, G, K, MG, MSE, U
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Overview

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.

About this Structure

1DUL is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of the ribonucleoprotein core of the signal recognition particle., Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA, Science. 2000 Feb 18;287(5456):1232-9. PMID:10678824

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