The use of double mutants to detect structural changes in the active site of the tyrosyl-tRNA synthetase (Bacillus stearothermophilus) (original) (raw)

Thermodynamic Analysis Reveals a Temperature-dependent Change in the Catalytic Mechanism of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase

Victor Ifeanyi

Journal of Biological Chemistry, 2008

Protein Engineering of Tyrosyl-tRNA Synthetase: The Charging of tRNA [and Discussion]

Phil. Trans. R. Soc. Lond. A: Mathematical, Physical and Engineering Sciences, 1986

Conformational Movements and Cooperativity upon Amino Acid, ATP and tRNA Binding in Threonyl-tRNA Synthetase

dino moras

Journal of Molecular Biology, 2003

Activation of D-Tyrosine by Bacillus stearothermophilus Tyrosyl-tRNA Synthetase: 1. PRE-STEADY-STATE KINETIC ANALYSIS REVEALS THE MECHANISTIC BASIS FOR THE RECOGNITION OF D-TYROSINE

Journal of Biological Chemistry, 2008

Correlations between kinetic and x-ray analyses of engineered enzymes: crystal structures of mutants Cys.fwdarw.Gly-35 and Tyr.fwdarw.Phe-34 of tyrosyl-tRNA synthetase

Alan Fersht

Biochemistry, 1991

Amino acid activation in crystalline tyrosyl-tRNA synthetase from Bacillus stearothermophilus

John Rubin

Journal of Molecular Biology, 1981

Mutational and kinetic analysis of a mobile loop in tyrosyl-tRNA synthetase

Biochemistry, 1993

Experimental evolution of a dense cluster of residues in tyrosyl-tRNA synthetase: quantitative effects on activity, stability and dimerization

Journal of Molecular Biology, 1999

Crystal Structure of Tryptophanyl-tRNA Synthetase Complexed with Adenosine-5′ Tetraphosphate: Evidence for Distributed Use of Catalytic Binding Energy in Amino Acid Activation by Class I Aminoacyl-tRNA Synthetases

Charles Carter

Journal of Molecular Biology, 2007

Interconversion of ATP Binding and Conformational Free Energies by Tryptophanyl-tRNA Synthetase: Structures of ATP Bound to Open and Closed

Charles Carter

2014

Interconversion of ATP Binding and Conformational Free Energies by Tryptophanyl-tRNA Synthetase: Structures of ATP Bound to Open and Closed, Pre-Transition-state Conformations

Valentin Ilyin

Journal of Molecular Biology, 2003

Correlating amino acid conservation with function in tyrosyl-tRNA synthetase 1 1 Edited by A. R. Fersht

J Mol Biol, 2000

Correlating amino acid conservation with function in tyrosyl-tRNA synthetase

Journal of Molecular Biology, 2000

A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

Stephane Commans

Biochemistry, 1995

Dimeric Tyrosyl-tRNA Synthetase from Bacillus stearothermophilus Unfolds through a Monomeric Intermediate: A Quantitative Analysis under Equilibrium Conditions.

Journal of Biological Chemistry, 1998

Structure and Dynamics of the Anticodon Arm Binding Domain of Bacillus stearothermophilus Tyrosyl-tRNA Synthetase

Muriel Delepierre, Iñaki Guijarro, Hugues Bedouelle

Structure, 2002

Distinct Steps in the Specific Binding of tRNA to Aminoacyl-tRNA Synthetase. Temperature-Jump Studies on the Serine-Specific System from Yeast and the Tyrosine-Specific System from Escherichia coli

Frens Peters

European Journal of Biochemistry, 1976

Induced Fit and Kinetic Mechanism of Adenylation Catalyzed by Escherichia coli Threonyl-tRNA Synthetase †

Christopher Francklyn

Biochemistry, 2003

Residues interacting with serine-174 and alanine-295 in the β-subunit of Escherichia coli H+ATP synthase: Possible ternary structure of the center region of the subunit

Yuri Ishihara

Biochimica Et Biophysica Acta-bioenergetics, 1994

Reconstruction by Site-Directed Mutagenesis of the Transition State for the Activation of Tyrosine by the Tyrosyl-tRNA Synthetase: A Mobile Loop Envelopes the Transition State in an Induced-Fit Mechanism

Biochemistry, 1988

Investigation of the ATP Binding Site of Escherichia coli Aminoimidazole Ribonucleotide Synthetase Using Affinity Labeling and Site-Directed Mutagenesis †

T. Kappock

Biochemistry, 1999

Comparison of the Catalytic Roles Played by the KMSKS Motif in the Human and Bacillus stearothermophilus Tyrosyl-tRNA Synthetases

Journal of Biological Chemistry, 2002

Effects of Substrate and Inhibitor Binding on Proteolysis of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Keith Moore

Journal of Biological Chemistry, 1998

Characterization of Isoleucyl-tRNA Synthetase from Staphylococcus aureus

Keith Moore

Journal of Biological Chemistry, 1998

Rational protein engineering in action: The first crystal structure of a phenylalanine tRNA synthetase from Staphylococcus haemolyticus

Lakshmi Narasimhan

Journal of Structural Biology, 2008

Affinity labeling of aminoacyl-tRNA synthetases with adenosine triphosphopyridoxal: Probing the Lys-Met-Ser-Lys-Ser signature sequence as the ATP-binding site in E. coli methionyl- and valyl-tRNA synthetases

Biochemistry, 1990

Affinity Labeling of Escherichia Coli Histidyl-tRNA Synthetase with Reactive ATP Analogues. Identification of Labeled Amino Acid Residues by Matrix Assisted Laser Desorption-Ionization Mass Spectrometry

European Journal of Biochemistry, 1996

E. coli tyrosyl- and methionyl-tRNA synthetases display sequence similarity at the binding site for the 3'-end of tRNA

Biochemistry, 1986

Trinitrophenyl-ATP and-ADP bind to a single nucleotide site on isolated beta-subunit of Escherichia coli F1-ATPase. In vitro assembly of F1-subunits requires …

Rajini Rao

Journal of Biological Chemistry, 1988

Manipulating the Length of the b Subunit F 1 Binding Domain in F 1 F 0 ATP Synthase from Escherichia coli

Tammy Grabar

Journal of Bioenergetics and Biomembranes, 2005

Nuclear overhauser effect studies of the conformations of MG(α, β-Methylene)ATP bound to E. coli isoleucyl-tRNA synthetase

Paul Rosevear

Biochemical and Biophysical Research Communications, 1991

Conformational changes in the Escherichia coli ATP synthase b-dimer upon binding to F1-ATPase

Tarek Zaida, Pia Vogel

Journal of Bioenergetics and Biomembranes, 2008

Primary Structure Revision and Active Site Mapping of E. Coli Isoleucyl-tRNA Synthetase by Means of Maldi Mass Spectrometry

The Open Biochemistry Journal, 2009

Transition state stabilization by the ‘high’ motif of class I aminoacyl-tRNA synthetases: the case of Escherichia coli methionyl-tRNA synthetase

Yves Mechulam

Nucleic Acids Research, 1995