(Q27641923)

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Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase

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scholarly article

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Use of analogues of methionine and methionyl adenylate to sample conformational changes during catalysis in Escherichia coli methionyl-tRNA synthetase (English)

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Escherichia coli

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author name string

Thibaut Crepin

1

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Emmanuelle Schmitt

2

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Yves Mechulam

3

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Peter B Sampson

4

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Mark D Vaughan

5

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John F Honek

6

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Sylvain Blanquet

7

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language of work or name

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publication date

5 September 2003

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number of pages

14

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Journal of Molecular Biology

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332

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1

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59-72

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Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

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Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases

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Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase

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

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A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.

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Aminoacylation error correction

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Enzyme structure with two catalytic sites for double-sieve selection of substrate

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tRNA aminoacylation by arginyl-tRNA synthetase: induced conformations during substrates binding

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Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase

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How methionyl-tRNA synthetase creates its amino acid recognition pocket upon L-methionine binding

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An editing mechanism for the methionyl-tRNA synthetase in the selection of amino acids in protein synthesis

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Alternative pathways for editing non-cognate amino acids by aminoacyl-tRNA synthetases

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Methionine in and out of proteins: targets for drug design

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Expanding the Scope of Protein Biosynthesis by Altering the Methionyl-tRNA Synthetase Activity of a Bacterial Expression Host Scott Ross was helpful in conducting the 1D TOCSY NMR experiments and Pratip Bhattachary is thanked for assistance in other

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Identification of an expanded set of translationally active methionine analogues in Escherichia coli

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Crystal structure of Escherichia coli methionyl-tRNA synthetase highlights species-specific features

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Vanilloid and isovanilloid analogues as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases

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Methionyl adenylate analogues as inhibitors of methionyl-tRNA synthetase

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Ester and hydroxamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases

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Optimisation of aryl substitution leading to potent methionyl tRNA synthetase inhibitors with excellent gram-positive antibacterial activity.

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Nanomolar inhibitors of Staphylococcus aureus methionyl tRNA synthetase with potent antibacterial activity against gram-positive pathogens.

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Aminoalkyl adenylate and aminoacyl sulfamate intermediate analogues differing greatly in affinity for their cognate Staphylococcus aureus aminoacyl tRNA synthetases

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The amino acid activation reaction catalyzed by methionyl-transfer RNA synthetase: Evidence for synergistic coupling between the sites for methionine adenosine and pyrophosphate

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N-Alkoxysulfamide, N-hydroxysulfamide, and sulfamate analogues of methionyl and isoleucyl adenylates as inhibitors of methionyl-tRNA and isoleucyl-tRNA synthetases

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Identification of residues involved in the binding of methionine by Escherichia coli methionyl-tRNA synthetase.

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10.1016/S0022-2836(03)00917-3

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