ArticleNature structural biology1997
Crystal structure of the EF-Tu.EF-Ts complex from Thermus thermophilus.
Article in Nature structural biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 119 citations in OpenAlex.
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- Tuning tRNAs for improved translation.Frontiers in genetics · 2024Review
- Structural insights of the elongation factor EF-Tu complexes in protein translation of Mycobacterium tuberculosis.Communications biology · 2022Article
- Functions and Regulation of Translation Elongation Factors.Frontiers in molecular biosciences · 2021Review
- Hybrid Structure of the RagA/C-Ragulator mTORC1 Activation Complex.Molecular cell · 2017Article
- Review: Translational GTPases.Biopolymers · 2016Review
- Evolutionary conservation and expression of human RNA-binding proteins and their role in human genetic disease.Advances in experimental medicine and biology · 2014Review
- Phosphoproteomic analysis reveals the effects of PilF phosphorylation on type IV pilus and biofilm formation in Thermus thermophilus HB27.Molecular & cellular proteomics : MCP · 2013Article
- Reconstitution of translation from Thermus thermophilus reveals a minimal set of components sufficient for protein synthesis at high temperatures and functional conservation of modern and ancient translation components.Nucleic acids research · 2012Article
- Molecular basis for RNA polymerization by Qβ replicase.Nature structural & molecular biology · 2012Article
- Cutaneous human papillomavirus type 38 E7 regulates actin cytoskeleton structure for increasing cell proliferation through CK2 and the eukaryotic elongation factor 1A.Journal of virology · 2011Article
- Conformational changes in redox pairs of protein structures.Protein science : a publication of the Protein Society · 2009Article
- Cofactor dependent conformational switching of GTPases.Biophysical journal · 2008Article
- Kinetics of the interactions between yeast elongation factors 1A and 1Balpha, guanine nucleotides, and aminoacyl-tRNA.The Journal of biological chemistry · 2007Article
- Phylogenetic distribution of translational GTPases in bacteria.BMC genomics · 2007Article
- Explanation of the stability of thermophilic proteins based on unique micromorphology.Biophysical journal · 2006Article
- Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.The EMBO journal · 2006Article
- Assessing functional divergence in EF-1alpha and its paralogs in eukaryotes and archaebacteria.Nucleic acids research · 2003Article
- Characterization of the interaction between the nucleotide exchange factor EF-Ts from nematode mitochondria and elongation factor Tu.Nucleic acids research · 2002Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In order to study nucleotide exchange mechanisms in GTP-binding proteins, we have determined the crystal structure of the complex formed by the elongation factor Tu (EF-Tu) and its exchange factor Ts (EF-Ts) from Thermus thermophilus. The complex is a dyad symmetrical heterotetramer in which each EF-Tu, through a bipartite interface, interacts with two subunits of EF-Ts, explaining the need for a dimeric exchange factor. The architecture of the assembly is distinctly different from that of the corresponding heterodimeric E. coli complex, in which the monomeric E. coli EF-Ts remarkably forms essentially the same bipartite interface with EF-Tu through a sequence/structural repeat. GDP is released primarily by a Ts-induced peptide flip in the nucleotide binding pocket that disrupts hydrogen bonds to the phosphates and repositions the peptide carbonyl so as to sterically and electrostatically eject the GDP. The exchange mechanism may have useful implications for receptor-induced exchange in heterotrimeric G proteins.
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