Transfer RNA-mediated editing in threonyl-tRNA synthetase: the class II solution to the double discrimination problem

Article Abstract:

Research reveals that wild-type and mutated versions of threonyl-tRNA synthetase bind serine and threonine similarly and use CCA and tRNA to switch between hairpin and a helical conformation during aminoacylation and editing.

United States, France, Statistical Data Included, Physiological aspects, Protein synthesis, Protein biosynthesis, Ligases, Amino acid structure-activity relationships

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Transmembrane signaling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes

Article Abstract:

A study was undertaken to determine the role of the ferric hydroxymate uptake protein component A (FhuA) in facilitating the ligand-gated transport of the siderophore ferrichrome. The structure of the protein revealed two domains and the binding site of the ferrichrome was at the apical interface of three turns of the plug domain and two loops of the barrel. The ferrichrome binding activated the interactions of the energy transducing TonB complex with the periplasmic surface of the FhuA protein.

Membrane proteins, Cellular signal transduction, Bacterial cell walls, Ligand binding (Biochemistry), Iron compounds

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The structure of threonyl-tRNA synthetase-tRNA(super Thr) complex enlightens its repressor activity and reveals an essential zinc ion in the active site

Article Abstract:

A study was conducted to examine the structure between Escherichia coli's transfer RNA (tRNA)(super Thr) and threonyl-tRNA synthetase. Results indicate that the threonyl-tRNA synthetase- complex has an amino-terminal domain that contains a novel protein fold that interacts with the tRNA acceptor stem. A zinc ion site was also found within the active site that induces amino acid recognition or discrimination.

Analysis, Escherichia coli, Aminoacyl-tRNA synthetases

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