ArticleStructure (London, England : 1993)2009
Mg2+-assisted catalysis by B. stearothermophilus TrpRS is promoted by allosteric effects.
Article in Structure (London, England : 1993), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 27 citations in OpenAlex.
- Microcalorimetry reveals multi-state thermal denaturation ofStructural dynamics (Melville, N.Y.) · 2023Article
- High-throughput thermal denaturation of tryptophanyl-tRNA synthetase combinatorial mutants reveals high-order energetic coupling determinants of conformational stability.Structural dynamics (Melville, N.Y.) · 2023Article
- Article
- High-Dimensional Mutant and Modular Thermodynamic Cycles, Molecular Switching, and Free Energy Transduction.Annual review of biophysics · 2017Review
- Combining multi-mutant and modular thermodynamic cycles to measure energetic coupling networks in enzyme catalysis.Structural dynamics (Melville, N.Y.) · 2017Article
- Augmenting the anisotropic network model with torsional potentials improves PATH performance, enabling detailed comparison with experimental rate data.Structural dynamics (Melville, N.Y.) · 2017Article
- Coding of Class I and II Aminoacyl-tRNA Synthetases.Advances in experimental medicine and biology · 2017Review
- An Ancestral Tryptophanyl-tRNA Synthetase Precursor Achieves High Catalytic Rate Enhancement without Ordered Ground-State Tertiary Structures.ACS chemical biology · 2016Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Selective Inhibition of Bacterial Tryptophanyl-tRNA Synthetases by Indolmycin Is Mechanism-based.The Journal of biological chemistry · 2016Article
- Urzymology: experimental access to a key transition in the appearance of enzymes.The Journal of biological chemistry · 2014Review
- Enhanced amino acid selection in fully evolved tryptophanyl-tRNA synthetase, relative to its urzyme, requires domain motion sensed by the D1 switch, a remote dynamic packing motif.The Journal of biological chemistry · 2014Article
- Full implementation of the genetic code by tryptophanyl-tRNA synthetase requires intermodular coupling.The Journal of biological chemistry · 2013Article
- Statistical evaluation of the Rodin-Ohno hypothesis: sense/antisense coding of ancestral class I and II aminoacyl-tRNA synthetases.Molecular biology and evolution · 2013Article
- Hyperconjugation-mediated solvent effects in phosphoanhydride bonds.The journal of physical chemistry. A · 2012Article
- A master switch couples Mg²⁺-assisted catalysis to domain motion in B. stearothermophilus tryptophanyl-tRNA Synthetase.Structure (London, England : 1993) · 2012Article
- Structure of Leishmania major methionyl-tRNA synthetase in complex with intermediate products methionyladenylate and pyrophosphate.Biochimie · 2011Article
- Tryptophanyl-tRNA synthetase Urzyme: a model to recapitulate molecular evolution and investigate intramolecular complementation.The Journal of biological chemistry · 2010Article
- Detection of native-state nonadditivity in double mutant cycles via hydrogen exchange.Journal of the American Chemical Society · 2010Article
- Crystal structures of Saccharomyces cerevisiae tryptophanyl-tRNA synthetase: new insights into the mechanism of tryptophan activation and implications for anti-fungal drug design.Nucleic acids research · 2010Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Mn(2+)-assisted catalysis by B. stearothermophilus TrpRS parallels that in polymerases and reduces specificity in amino acid activation. As predicted by nonequilibrium molecular dynamics simulations, multivariant thermodynamic cycles with [ATP]-dependent Michaelis-Menten kinetics and Mn(2+) for Mg(2+) substitution demonstrate energetic coupling of ATP affinities to the metal; to lysines K111 and K192, which interact via the PPi leaving group; and to K195, which couples differently to the metal via the alpha-phosphate. However, net coupling to the metal opposes catalysis in both ground (K(M)) and transition (k(cat)) states. The 10(5)-fold rate acceleration by Mg(2+)-protein interactions therefore requires additional favorable protein-metal couplings. Examples include longer-range, i.e., allosteric, interactions previously illustrated by the remote F37I mutation, which both reduces k(cat) and enhances catalytic assist by Mn(2+), relative to that by Mg(2+). These data support a model linking metal-assisted phosphoryl transfer catalysis to domain movement, and hence to free-energy transduction in a broad range of enzymes.
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