Yeast Phenylalanyl-tRNA Synthetase. Stoichiometry of the Phenylalanyl Adenylate . Enzyme Complex and Transfer of Phenylalanine from this Complex to tRNAPhe
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چکیده
منابع مشابه
Phenylalanyl-tRNA synthetase from baker's yeast: structural organization of the enzyme and its complex with tRNAPhe as determined by X-ray small-angle scattering.
The quaternary structure of the phenylalanyl-tRNA synthetase and its complex with tRNAPhe was studied in dilute solutions by small angle X-ray scattering. For the free synthetase the radius of gyration was determined as 5.5 nm, the volume 523 nm3, the maximum diameter 17.5 nm and the molecular weight as 260,000 using an isopotential specific volume of 0.735. The overall shape could be best appr...
متن کاملCrystal Structure at 2.6Å Resolution of Phenylalanyl-tRNA Synthetase Complexed with Phenylalanyl-Adenylate in the Presence of Manganese Ions
Introduction: Aminoacyl-tRNA synthetases (aaRSs) is a family of enzymes, that covalently attach amino acids to a cognate tRNAs through a two-step aminoacylation reaction. At the first step, amino acid is activated by the attack of ATP molecule, giving rise to an intermediate molecule, aminoacyl-adenylate. Based on their structural and functional features, aaRSs are divided into two classes. Phe...
متن کاملVirtual screening for binding of phenylalanine analogues to phenylalanyl-tRNA synthetase.
Although incorporation of nonnatural amino acids provides a powerful means of controlling protein structure and function, experimental investigations of amino acid analogues for utilization by the protein biosynthetic machinery can be costly and time-consuming. In this paper, we describe a computational protocol (HierDock) for predicting the relative energies of binding of phenylalanine analogu...
متن کاملPost-transfer editing in vitro and in vivo by the beta subunit of phenylalanyl-tRNA synthetase.
Translation of the genetic code requires attachment of tRNAs to their cognate amino acids. Errors during amino-acid activation and tRNA esterification are corrected by aminoacyl-tRNA synthetase-catalyzed editing reactions, as extensively described for aliphatic amino acids. The contribution of editing to aromatic amino-acid discrimination is less well understood. We show that phenylalanyl-tRNA ...
متن کاملEscherichia coli mutants overproducing phenylalanyl- and threonyl-tRNA synthetase.
The structural genes for threonyl-tRNA synthetase (ThrRS) and phenylalanyl-tRNA synthetase (PheRS) are closely linked on the Escherichia coli chromosome. To study whether these enzymes share a common regulatory element, we have investigated their synthesis in mutants which were selected for overproduction of either ThrRS or PheRS. It was found that mutants isolated previously for overproduction...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1974
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1974.tb03830.x