Summary information and primary citation
- PDB-id
-
1dul;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- signaling protein-RNA
- Method
- X-ray (1.8 Å)
- Summary
- Structure of the ribonucleoprotein core of the e. coli
signal recognition particle
- Reference
-
Batey RT, Rambo RP, Lucast L, Rha B, Doudna JA (2000):
"Crystal
structure of the ribonucleoprotein core of the signal
recognition particle." Science,
287, 1232-1239. doi: 10.1126/science.287.5456.1232.
- 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.
