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1l9a
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(New page: 200px<br /> <applet load="1l9a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l9a, resolution 2.90Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 15:51, 12 November 2007
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CRYSTAL STRUCTURE OF SRP19 IN COMPLEX WITH THE S DOMAIN OF SIGNAL RECOGNITION PARTICLE RNA
Overview
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.
About this Structure
1L9A is a Protein complex structure of sequences from Methanocaldococcus jannaschii with MG and MMC as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of SRP19 in complex with the S domain of SRP RNA and its implication for the assembly of the signal recognition particle., Oubridge C, Kuglstatter A, Jovine L, Nagai K, Mol Cell. 2002 Jun;9(6):1251-61. PMID:12086622
Page seeded by OCA on Mon Nov 12 17:57:57 2007
