Summary information and primary citation
- PDB-id
-
1l9a;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- signaling protein-RNA
- Method
- X-ray (2.9 Å)
- Summary
- Crystal structure of srp19 in complex with the s domain
of signal recognition particle RNA
- Reference
-
Oubridge C, Kuglstatter A, Jovine L, Nagai K (2002):
"Crystal
structure of SRP19 in complex with the S domain of SRP
RNA and its implication for the assembly of the signal
recognition particle." Mol.Cell,
9, 1251-1261. doi: 10.1016/S1097-2765(02)00530-0.
- Abstract
- The signal recognition particle (SRP) is a
ribonucleoprotein particle involved in GTP-dependent
translocation of secretory proteins across membranes. In
Archaea and Eukarya, SRP19 binds to 7SL RNA and promotes
the incorporation of SRP54, which contains the binding
sites for GTP, the signal peptide, and the membrane-bound
SRP receptor. We have determined the crystal structure of
Methanococcus jannaschii SRP19 bound to the S domain of
human 7SL RNA at 2.9 A resolution. SRP19 clamps the
tetraloops of two branched helices (helices 6 and 8) and
allows them to interact side by side. Helix 6 acts as a
splint for helix 8 and partially preorganizes the binding
site for SRP54 in helix 8, thereby facilitating the binding
of SRP54 in assembly.
