ArticleJournal of structural biology2007
Structure of the GMPPNP-stabilized NG domain complex of the SRP GTPases Ffh and FtsY.
Article in Journal of structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Structure of the GDP-bound state of the SRP GTPase FlhF.Acta crystallographica. Section F, Structural biology communications · 2024Article
- Article
- Structures of the E. coli translating ribosome with SRP and its receptor and with the translocon.Nature communications · 2016Article
- 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
- Signal recognition particle: an essential protein-targeting machine.Annual review of biochemistry · 2013Review
- The crystal structure of the signal recognition particle in complex with its receptor.Science (New York, N.Y.) · 2011Article
- Lipid activation of the signal recognition particle receptor provides spatial coordination of protein targeting.The Journal of cell biology · 2010Article
- 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
- SRP RNA controls a conformational switch regulating the SRP-SRP receptor interaction.Nature structural & molecular biology · 2008Article
- Article
- Article
- Minimizing frustration by folding in an aqueous environment.Archives of biochemistry and biophysics · 2008Article
- 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
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ffh and FtsY are GTPase components of the signal recognition particle co-translational targeting complex that assemble during the SRP cycle to form a GTP-dependent and pseudo twofold symmetric heterodimer. Previously the SRP GTPase heterodimer has been stabilized and purified for crystallographic studies using both the non-hydrolysable GTP analog GMPPCP and the pseudo-transition state analog GDP:AlF4, revealing in both cases a buried nucleotide pair that bridges and forms a key element of the heterodimer interface. A complex of Ffh and FtsY from Thermus aquaticus formed in the presence of the analog GMPPNP could not be obtained, however. The origin of this failure was previously unclear, and it was thought to have arisen from either instability of the analog, or, alternatively, from differences in its interactions within the tightly conscribed composite active site chamber of the complex. Using insights gained from the previous structure determinations, we have now determined the structure of the SRP GTPase targeting heterodimer stabilized by the non-hydrolysable GTP analog GMPPNP. The structure demonstrates how the different GTP analogs are accommodated within the active site chamber despite slight differences in the geometry of the phosphate chain. It also reveals a K+ coordination site at the highly conserved DARGG loop at the N/G interdomain interface.
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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.