1L9A

CRYSTAL STRUCTURE OF SRP19 IN COMPLEX WITH THE S DOMAIN OF SIGNAL RECOGNITION PARTICLE RNA

Summary for 1L9A

• Entry DOI: 10.2210/pdb1l9a/pdb
• Descriptor: signal recognition particle RNA S domain, SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: protein-rna complex, ribonucleoprotein, srp, signal recognition particle, tetraloop, signaling protein-rna complex, signaling protein/rna
• Biological source: Methanocaldococcus jannaschii; More
• Total number of polymer chains: 2
• Total formula weight: 52707.01

Authors

Oubridge, C.,Kuglstatter, A.,Jovine, L.,Nagai, K. (deposition date: 2002-03-22, release date: 2002-06-28, Last modification date: 2024-02-14)

Primary citation

Oubridge, C.,Kuglstatter, A.,Jovine, L.,Nagai, K.
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, 2002

PubMed 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.

PubMed: 12086622
DOI: 10.1016/S1097-2765(02)00530-0

Experimental method

X-RAY DIFFRACTION (2.9 Å)