ArticleProceedings of the National Academy of Sciences of the United States of America2003
Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 99 citations in OpenAlex.
- Molecular Characterization of Tc964, A Novel Antigenic Protein fromInternational journal of molecular sciences · 2020Article
- Reconstitution of the human SRP system and quantitative and systematic analysis of its ribosome interactions.Nucleic acids research · 2019Article
- The Archaeal Signal Recognition Particle: Present Understanding and Future Perspective.Current microbiology · 2017Review
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Domain Organization in the 54-kDa Subunit of the Chloroplast Signal Recognition Particle.Biophysical journal · 2016Article
- Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.Nature communications · 2016Article
- Dynamics of co-translational protein targeting.Current opinion in chemical biology · 2015Review
- Noncanoncial signal recognition particle RNAs in a major eukaryotic phylum revealed by purification of SRP from the human pathogen Cryptococcus neoformans.Nucleic acids research · 2015Article
- Article
- Signal-sequence induced conformational changes in the signal recognition particle.Nature communications · 2015Article
- Ribosome-SRP-FtsY cotranslational targeting complex in the closed state.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Allosteric response and substrate sensitivity in peptide binding of the signal recognition particle.The Journal of biological chemistry · 2014Article
- Co-translational protein targeting to the bacterial membrane.Biochimica et biophysica acta · 2014Review
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- RNA gymnastics in mammalian signal recognition particle assembly.RNA biology · 2014Article
- Endoplasmic reticulum targeting and insertion of tail-anchored membrane proteins by the GET pathway.Cold Spring Harbor perspectives in biology · 2013Review
- Structural basis of signal sequence surveillance and selection by the SRP-FtsY complex.Nature structural & molecular biology · 2013Article
- Protein translocation across the rough endoplasmic reticulum.Cold Spring Harbor perspectives in biology · 2013Review
- Fingerloop activates cargo delivery and unloading during cotranslational protein targeting.Molecular biology of the cell · 2013Article
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Targeting of secretory and membrane proteins by the signal recognition particle (SRP) is evolutionarily conserved, and the multidomain protein SRP54 acts as the key player in SRP-mediated protein transport. Binding of a signal peptide to SRP54 at the ribosome is coordinated with GTP binding and subsequent complex formation with the SRP receptor. Because these functions are localized to distinct domains of SRP54, communication between them is essential. We report the crystal structures of SRP54 from the Archaeon Sulfolobus solfataricus with and without its cognate SRP RNA binding site (helix 8) at 4-A resolution. The two structures show the flexibility of the SRP core and the position of SRP54 relative to the RNA. A long linker helix connects the GTPase (G domain) with the signal peptide binding (M) domain, and a hydrophobic contact between the N and M domains relates the signal peptide binding site to the G domain. Hinge regions are identified in the linker between the G and M domains (292-LGMGD) and in the N-terminal part of the M domain, which allow for structural rearrangements within SRP54 upon signal peptide binding at the ribosome.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.