ArticleJournal of molecular biology2002
Structural basis for mobility in the 1.1 A crystal structure of the NG domain of Thermus aquaticus Ffh.
Article in Journal of molecular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
17 citing papers in PubMed, 36 citations in OpenAlex.
- Structure of GPN-Loop GTPase Npa3 and Implications for RNA Polymerase II Assembly.Molecular and cellular biology · 2015Article
- HorA web server to infer homology between proteins using sequence and structural similarity.Nucleic acids research · 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
- Review
- Interaction of signal-recognition particle 54 GTPase domain and signal-recognition particle RNA in the free signal-recognition particle.Proceedings of the National Academy of Sciences of the United States of America · 2007Article
- 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
- 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
- Domain motions of glucosamine-6P synthase: comparison of the anisotropic displacements in the crystals and the catalytic hinge-bending rotation.Protein science : a publication of the Protein Society · 2007Article
- Analysis of protein hydration in ultrahigh-resolution structures of the SRP GTPase Ffh.Acta crystallographica. Section D, Biological crystallography · 2006Article
- Structure of a GDP:AlF4 complex of the SRP GTPases Ffh and FtsY, and identification of a peripheral nucleotide interaction site.Journal of molecular biology · 2006Article
- Article
- Heterodimeric GTPase core of the SRP targeting complex.Science (New York, N.Y.) · 2004Article
- Crystal structure of the complete core of archaeal signal recognition particle and implications for interdomain communication.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.Acta crystallographica. Section D, Biological crystallography · 2003Article
- Structure, function and evolution of the signal recognition particle.The EMBO journal · 2003Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
The NG domain of the prokaryotic signal recognition protein Ffh is a two-domain GTPase that comprises part of the prokaryotic signal recognition particle (SRP) that functions in co-translational targeting of proteins to the membrane. The interface between the N and G domains includes two highly conserved sequence motifs and is adjacent in sequence and structure to one of the conserved GTPase signature motifs. Previous structural studies have shown that the relative orientation of the two domains is dynamic. The N domain of Ffh has been proposed to function in regulating the nucleotide-binding interactions of the G domain. However, biochemical studies suggest a more complex role for the domain in integrating communication between signal sequence recognition and interaction with receptor. Here, we report the structure of the apo NG GTPase of Ffh from Thermus aquaticus refined at 1.10 A resolution. Although the G domain is very well ordered in this structure, the N domain is less well ordered, reflecting the dynamic relationship between the two domains previously inferred. We demonstrate that the anisotropic displacement parameters directly visualize the underlying mobility between the two domains, and present a detailed structural analysis of the packing of the residues, including the critical alpha4 helix, that comprise the interface. Our data allows us to propose a structural explanation for the functional significance of sequence elements conserved at the N/G interface.
Indexed as
Identifiers
What OpenQuestion holds
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.