ArticleProteins2007
X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.
Article in Proteins, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Structure of the GDP-bound state of the SRP GTPase FlhF.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- ATPase and GTPase Tangos Drive Intracellular Protein Transport.Trends in biochemical sciences · 2016Review
- Fidelity of cotranslational protein targeting by the signal recognition particle.Annual review of biophysics · 2014Review
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
- Signal recognition particle (SRP) and SRP receptor: a new paradigm for multistate regulatory GTPases.Biochemistry · 2009Article
- The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.The Journal of biological chemistry · 2009Article
- Nucleotide-binding flexibility in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2008Article
- 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
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- The crystal structure of the third signal-recognition particle GTPase FlhF reveals a homodimer with bound GTP.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.PloS one · 2007Article
- Efficient interaction between two GTPases allows the chloroplast SRP pathway to bypass the requirement for an SRP RNA.Molecular biology of the cell · 2007Article
- Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.Journal of structural biology · 2007Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
FtsY and Ffh are structurally similar prokaryotic Signal Recognition Particle GTPases that play an essential role in the Signal Recognition Particle (SRP)-mediated cotranslational targeting of proteins to the membrane. The two GTPases assemble in a GTP-dependent manner to form a heterodimeric SRP targeting complex. We report here the 2.1 A X-ray structure of FtsY from T. aquaticus bound to GDP. The structure of the monomeric protein reveals, unexpectedly, canonical binding interactions for GDP. A comparison of the structures of the monomeric and complexed FtsY NG GTPase domain suggests that it undergoes a conformational change similar to that of Ffh NG during the assembly of the symmetric heterodimeric complex. However, in contrast to Ffh, in which the C-terminal helix shifts independently of the other subdomains, the C-terminal helix and N domain of T. aquaticus FtsY together behave as a rigid body during assembly, suggesting distinct mechanisms by which the interactions of the NG domain "module" are regulated in the context of the two SRP GTPases.
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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.