ArticleJournal of molecular biology2006
Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site.
Article in Journal of molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
- Common Mechanism of Activated Catalysis in P-loop Fold Nucleoside Triphosphatases-United in Diversity.Biomolecules · 2022Article
- Structure of the quaternary complex between SRP, SR, and translocon bound to the translating ribosome.Nature communications · 2017Article
- The structural basis of FtsY recruitment and GTPase activation by SRP RNA.Molecular cell · 2013Article
- Structural basis for the molecular evolution of SRP-GTPase activation by protein.Nature structural & molecular biology · 2011Article
- Direct visualization reveals dynamics of a transient intermediate during protein assembly.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The crystal structure of the signal recognition particle in complex with its receptor.Science (New York, N.Y.) · 2011Article
- Transient tether between the SRP RNA and SRP receptor ensures efficient cargo delivery during cotranslational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- It takes two to tango: regulation of G proteins by dimerization.Nature reviews. Molecular cell biology · 2009Review
- Multiple conformational switches in a GTPase complex control co-translational protein targeting.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Demonstration of a multistep mechanism for assembly of the SRP x SRP receptor complex: implications for the catalytic role of SRP RNA.Journal of molecular biology · 2008Article
- SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Nature structural & molecular biology · 2008Article
- Structure of the Roc-COR domain tandem of C. tepidum, a prokaryotic homologue of the human LRRK2 Parkinson kinase.The EMBO journal · 2008Article
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- X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.PloS one · 2007Article
- Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.Journal of structural biology · 2007Article
- X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.Proteins · 2007Article
- SRP RNA provides the physiologically essential GTPase activation function in cotranslational protein targeting.RNA (New York, N.Y.) · 2007Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The signal recognition particle (SRP) GTPases Ffh and FtsY play a central role in co-translational targeting of proteins, assembling in a GTP-dependent manner to generate the SRP targeting complex at the membrane. A suite of residues in FtsY have been identified that are essential for the hydrolysis of GTP that accompanies disengagement. We have argued previously on structural grounds that this region mediates interactions that serve to activate the complex for disengagement and term it the activation region. We report here the structure of a complex of the SRP GTPases formed in the presence of GDP:AlF4. This complex accommodates the putative transition-state analog without undergoing significant change from the structure of the ground-state complex formed in the presence of the GTP analog GMPPCP. However, small shifts that do occur within the shared catalytic chamber may be functionally important. Remarkably, an external nucleotide interaction site was identified at the activation region, revealed by an unexpected contaminating GMP molecule bound adjacent to the catalytic chamber. This site exhibits conserved sequence and structural features that suggest a direct interaction with RNA plays a role in regulating the activity of the SRP targeting complex.
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Registered trials
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.