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: 2024-11-20) |
| 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 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: 10678824DOI: 10.1126/science.287.5456.1232 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
