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Escherichia coli Leucyl-tRNA Synthetase †
, 2000
"... ABSTRACT: Leucyl-tRNA synthetase (LeuRS) is a class I aminoacyl-tRNA synthetase that catalyzes leucylation of tRNA Leu. Several mutants in the CP1 domain of Escherichia coli LeuRS were obtained by introduction of restriction endonuclease sites into its gene, leuS. Of these mutants, only LeuRS-A293F ..."
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ABSTRACT: Leucyl-tRNA synthetase (LeuRS) is a class I aminoacyl-tRNA synthetase that catalyzes leucylation of tRNA Leu. Several mutants in the CP1 domain of Escherichia coli LeuRS were obtained by introduction of restriction endonuclease sites into its gene, leuS. Of these mutants, only LeuRS-A293F
The Crystallization of Ribosomal Proteins from the 50 S Subunit of the Escherichia coli and Bacillus stearothermophilus Ribosome*
"... Several individual intact ribosomal proteins purified from bacterial sources under mild conditions have been crystallized. A number of these are suitable candidates for three-dimensional structural studies b x-ray dif-fraction techniques. Data collection to 3 J resolution for one of these proteins i ..."
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of the ribosome structure at he molecular level. The success achieved in identifying function within the structures of many globular proteins, notably enzymes (1,2), encourages a similar approach to this more complex system.
CP1 domain in Escherichia coli leucyl-tRNA synthetase is crucial for its editing function, Biochemistry 39
, 2000
"... ABSTRACT: The amino acid discrimination by aminoacyl-tRNA synthetase is achieved through two sifting steps; amino acids larger than the cognate substrate are rejected by a “coarse sieve”, while the reaction products of amino acids smaller than the cognate substrate will go through a “fine sieve ” an ..."
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Cited by 31 (13 self)
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” and be hydrolyzed. This “double-sieve ” mechanism has been proposed for IleRS, a class I aminoacyl-tRNA synthetase. In this study, we created LeuRS-B, a mutant leucyl-tRNA synthetase from Escherichia coli with a duplication of the peptide fragment from Met328 to Pro368 (within its CP1 domain). This mutant has 50
Copyright © 1997, American Society for Microbiology Characterization of a Thermosensitive Escherichia coli Aspartyl-tRNA Synthetase Mutant
, 1996
"... The Escherichia coli tls-1 strain carrying a mutated aspS gene (coding for aspartyl-tRNA synthetase), which causes a temperature-sensitive growth phenotype, was cloned by PCR, sequenced, and shown to contain a single mutation resulting in substitution by serine of the highly conserved proline 555, w ..."
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The Escherichia coli tls-1 strain carrying a mutated aspS gene (coding for aspartyl-tRNA synthetase), which causes a temperature-sensitive growth phenotype, was cloned by PCR, sequenced, and shown to contain a single mutation resulting in substitution by serine of the highly conserved proline 555
Aminoacyl-tRNA Synthetase Have a Common Epitope Which Maps to the Catalytic Domain of Each*
"... We report here the identification of a common immunological determinant in Escherichia coli and Bom-byx mori (silkworm) alanine tRNA synthetases. The E. coli protein is a tetramer of identical M, = 95,000 chains, and the silkworm enzyme is a monomer of M, = 115,000. Antibodies against the silkworm ..."
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We report here the identification of a common immunological determinant in Escherichia coli and Bom-byx mori (silkworm) alanine tRNA synthetases. The E. coli protein is a tetramer of identical M, = 95,000 chains, and the silkworm enzyme is a monomer of M, = 115,000. Antibodies against the silkworm
ORIGINAL PAPER Probing the global and local dynamics of aminoacyl-tRNA synthetases using all-atom and coarse-grained simulations
"... Abstract Coarse-grained simulations have emerged as in-valuable tools for studying conformational changes in biomol-ecules. To evaluate the effectiveness of computationally inex-pensive coarse-grained models in studying global and local dynamics of large protein systems like aminoacyl-tRNA syn-theta ..."
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, we have performed coarse-grained normal mode analysis, as well as principle component analysis on trajecto-ries of all-atom and coarse-grained molecular dynamics sim-ulations for three aminoacyl-tRNA synthetases—Escherichia coli methionyl-tRNA synthetase, Thermus thermophilus leucyl-tRNA synthetase
Printed in (~s.A. Two Mutations in the Dispensable Part of Alanine tRNA Synthetase Which Affect the Catalytic Activity*
"... Two previously described chromosomal mutant al- been characterized at the level of protein primary structure leles, daS4 and daS5, of Escherichia coli Ala-tRNA and interpreted within the framework of the previously synthetase have been analyzed. Each causes a sharp mapped functional domains. This is ..."
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Two previously described chromosomal mutant al- been characterized at the level of protein primary structure leles, daS4 and daS5, of Escherichia coli Ala-tRNA and interpreted within the framework of the previously synthetase have been analyzed. Each causes a sharp mapped functional domains
Evolving strategies for enzyme engineering.
- Curr. Opin. Struct. Biol.
, 2005
"... Directed evolution is a common technique to engineer enzymes for a diverse set of applications. Structural information and an understanding of how proteins respond to mutation and recombination are being used to develop improved directed evolution strategies by increasing the probability that mutan ..."
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Cited by 18 (0 self)
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bond formation system in Escherichia coli Schultz and co-workers have created tRNA synthetases that charge orthogonal tRNAs with non-natural amino acids by targeting mutagenesis to five or six amino acids involved in substrate recognition. They then performed a positive selection for recognition
LETTER TO THE EDITOR Aminoacylated tmRNA from Escherichia coli interacts with prokaryotic elongation factor Tu
"... they function, at least in Escherichia coli, both as tRNA and mRNA (for a review, see Muto et al+, 1998)+ These;360 6 40-nt-long RNAs are charged with alanine at their 39 ends by alanyl-tRNA synthetases or AlaRS (Komine et al+, 1994; Ushida et al+, 1994)+ Alanylation occurs thanks to the presence of ..."
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they function, at least in Escherichia coli, both as tRNA and mRNA (for a review, see Muto et al+, 1998)+ These;360 6 40-nt-long RNAs are charged with alanine at their 39 ends by alanyl-tRNA synthetases or AlaRS (Komine et al+, 1994; Ushida et al+, 1994)+ Alanylation occurs thanks to the presence
tRNA-Modifying Enzyme tRNA±Guanine Trans- glycosylase and Their Implications for Substrate Selectivity, Reaction Mechanism and Structure- Based Drug Design
"... catalyses a base-exchange reaction that leads to anticodon modifications of certain tRNAs. The TGT enzymes of the eubacteria Zymomonas mobilis (Z. mobilis TGT) and Escherichia coli (E. co-li TGT) show a different behaviour in the presence of competitive inhibitors. The active sites of both enzymes a ..."
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catalyses a base-exchange reaction that leads to anticodon modifications of certain tRNAs. The TGT enzymes of the eubacteria Zymomonas mobilis (Z. mobilis TGT) and Escherichia coli (E. co-li TGT) show a different behaviour in the presence of competitive inhibitors. The active sites of both enzymes
Results 1 - 10
of
20
