About: T arm is a research topic. Over the lifetime, 883 publications have been published within this topic receiving 54105 citations. The topic is also known as: T-loop.
TL;DR: The crystal structure of the complete Thermus thermophilus 70S ribosome containing bound messenger RNA and transfer RNAs (tRNAs) at 5.5 angstrom resolution is described, suggesting coupling of the 20 to 50 angstrom movements associated with tRNA translocation with intersubunit movement.
Abstract: We describe the crystal structure of the complete Thermus thermophilus 70S ribosome containing bound messenger RNA and transfer RNAs (tRNAs) at 5.5 angstrom resolution. All of the 16S, 23S, and 5S ribosomal RNA (rRNA) chains, the A-, P-, and E-site tRNAs, and most of the ribosomal proteins can be fitted to the electron density map. The core of the interface between the 30S small subunit and the 50S large subunit, where the tRNA substrates are bound, is dominated by RNA, with proteins located mainly at the periphery, consistent with ribosomal function being based on rRNA. In each of the three tRNA binding sites, the ribosome contacts all of the major elements of tRNA, providing an explanation for the conservation of tRNA structure. The tRNAs are closely juxtaposed with the intersubunit bridges, in a way that suggests coupling of the 20 to 50 angstrom movements associated with tRNA translocation with intersubunit movement.
TL;DR: The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (t RNA) and metal ions also stabilize the intersubunit interface.
Abstract: The crystal structure of the bacterial 70S ribosome refined to 2.8 angstrom resolution reveals atomic details of its interactions with messenger RNA (mRNA) and transfer RNA (tRNA). A metal ion stabilizes a kink in the mRNA that demarcates the boundary between A and P sites, which is potentially important to prevent slippage of mRNA. Metal ions also stabilize the intersubunit interface. The interactions of E-site tRNA with the 50S subunit have both similarities and differences compared to those in the archaeal ribosome. The structure also rationalizes much biochemical and genetic data on translation.
TL;DR: The tRNA identity problem: past, present and future Small RNA oligonucleotide substrates for specific aminoacylations tRNA discrimination in aminoacylation Recognition in the glutamine tRNA system: from structure to function
Abstract: Transfer RNA after four decades tRNA: discovery, early work and total synthesis of tRNA genes Structure and expression of prokaryotic tRNA genes Transcription of eukaryotic tRNA genes tRNA processing nucleases Recent studies of RNase P Splicing of tRNA precursors Primary, secondary and tertiary structure of tRNAs Organellar tRNAs: biosynthesis and function tRNA-like structures in plant viral RNAs Biosynthesis and function of modified nucleosides Modified nucleosides and codon recognition tRNA sequences and variations in the genetic code Aminoacyl-tRNA synthetases: occurrence, structure and function Bacterial aminoacyl-tRNA synthetases: genes and regulation of expression The tRNA identity problem: past, present and future Small RNA oligonucleotide substrates for specific aminoacylations tRNA discrimination in aminoacylation Recognition in the glutamine tRNA system: from structure to function The aspartic acid tRNA system: recognition by a class II aminoacyl-tRNA synthetase Recognition of aminoacyl-tRNAs by protein elongatin factors tRNA on the ribosome: a waggle theory Discontinuous triplet decoding with or without re-pairing by peptidyl tRNA Translational suppression: when two wrongs do make a right Initiator tRNAs and initiation of protein synthesis The selenocysteine-inserting tRNA species: structure and function Glutamyl-tRNA as an intermediate in glutamate conversions
TL;DR: Direct chemical 'footprinting' shows that translocation of transfer RNA occurs in two discrete steps, and the acceptor end of tRNA moves relative to the large ribosomal subunit resulting in 'hybrid states' of binding.
Abstract: Direct chemical 'footprinting' shows that translocation of transfer RNA occurs in two discrete steps. During the first step, which occurs spontaneously after the formation of the peptide bond, the acceptor end of tRNA moves relative to the large ribosomal subunit resulting in 'hybrid states' of binding. During the second step, which is promoted by elongation factor EF-G, the anticodon end of tRNA, along with the messenger RNA, moves relative to the small ribosomal subunit.
TL;DR: In this article, crystal structures of the 30S ribosomal subunit with codon and near-cognate tRNA anticodon stem loops bound at decoding center and compare affinities of equivalent complexes in solution were reported.