The structure of the ternary complex consisting of yeast phenylalanyl-transfer RNA (Phe-
tRNAPhe), Thermus aquaticus elongation factor Tu (EF-Tu), and the guanosine triphosphate …

Background: Elongation factor Tu (EF-Tu) is a GTP-binding protein that is crucial for protein
biosynthesis. In the GTP form of the molecule, EF-Tu binds tightly to aminoacyl-tRNA …

Background: The translation elongation factor EF-Tu in its GTP-bound state forms a ternary
complex with any aminoacylated tRNA (aa-tRNA), except initiator tRNA and selenocysteinyl …

The machinery of eukaryotic protein synthesis is found in association with the actin
cytoskeleton. A major component of this translational apparatus, which is involved in the …

Comparative sequence analyses were performed on 14 genes encoding bacterial
elongation factors EF-Tu and 7 genes encoding the β-subunit of bacterial F 1 F 0 type ATP …

Advances in high-throughput sequencing have increased the availability of microbiome
sequencing data that can be exploited to characterize microbiome community structure in …

Prokaryotic elongation factors EF-Tu form a family of homologous, three-domain molecular
switches catalyzing the binding of aminoacyl-tRNAs to ribosomes during the process of …

The G domain and domain II in the crystal structure of Thermus thermophilus elongation
factor G (EF-G) were compared with the homologous domains in Thermus aquaticus …

The conformation of mammalian elongation factor eEF1A in solution was examined by the
small angle neutron scattering and scanning microcalorimetry. We have found that in …

A 6‐kb DNA fragment from an extreme thermophile, Thermus thermophilus, carrying the
genes for cytochrome oxidase ba3 subunit I (cbaA) and the ribosomal protein S15 (rpsO) …