2v3c
From Proteopedia
|
CRYSTAL STRUCTURE OF THE SRP54-SRP19-7S.S SRP RNA COMPLEX OF M. JANNASCHII
Overview
The signal-recognition particle (SRP) is a ubiquitous protein-RNA complex, that targets proteins to cellular membranes for insertion or secretion. A, key player in SRP-mediated protein targeting is the evolutionarily, conserved core consisting of the SRP RNA and the multidomain protein, SRP54. Communication between the SRP54 domains is critical for SRP, function, where signal sequence binding at the M domain directs receptor, binding at the GTPase domain (NG domain). These SRP activities are linked, to domain rearrangements, for which the role of SRP RNA is not clear. In, free SRP, a direct interaction of the GTPase domain with SRP RNA has been, proposed but has never been structurally verified. In this study, we, present the crystal structure at 2.5-A resolution of the SRP54-SRP19-SRP, RNA complex of Methanococcus jannaschii SRP. The structure reveals an, RNA-bound conformation of the SRP54 GTPase domain, in which the domain is, spatially well separated from the signal peptide binding site. The, association of both the N and G domains with SRP RNA in free SRP provides, further structural evidence for the pivotal role of SRP RNA in the, regulation of the SRP54 activity.
About this Structure
2V3C is a Protein complex structure of sequences from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.
Reference
Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle., Hainzl T, Huang S, Sauer-Eriksson AE, Proc Natl Acad Sci U S A. 2007 Sep 18;104(38):14911-6. Epub 2007 Sep 10. PMID:17846429
Page seeded by OCA on Wed Jan 23 13:08:26 2008
