2V3C

Crystal structure of the SRP54-SRP19-7S.S SRP RNA complex of M. jannaschii

Summary for 2V3C

• Entry DOI: 10.2210/pdb2v3c/pdb
• Related: 1L9A 1LNG
• Descriptor: SIGNAL RECOGNITION PARTICLE 19 KDA PROTEIN, SIGNAL RECOGNITION 54 KDA PROTEIN, 7S RNA, ... (4 entities in total)
• Functional Keywords: nucleotide-binding, signal recognition particle, rna, gtp-binding, rna-binding, ribonucleoprotein, signaling protein
• Biological source: METHANOCALDOCOCCUS JANNASCHII; More
• Cellular location: Cytoplasm (By similarity): Q58440
• Total number of polymer chains: 6
• Total formula weight: 179462.75

Authors

Hainzl, T.,Huang, S.,Sauer-Eriksson, A.E. (deposition date: 2007-06-15, release date: 2007-09-04, Last modification date: 2023-12-13)

Primary citation

Hainzl, T.,Huang, S.,Sauer-Eriksson, A.E.
Interaction of Signal-Recognition Particle 54 Gtpase Domain and Signal-Recognition Particle RNA in the Free Signal-Recognition Particle.
Proc.Natl.Acad.Sci.USA, 104:14911-, 2007

PubMed Abstract: 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.

PubMed: 17846429
DOI: 10.1073/PNAS.0702467104

Experimental method

X-RAY DIFFRACTION (2.5 Å)