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© Structural Dynamics Of Macromolecules
The structure of a bacterial analog of the nicotinic receptor (one color per subunit) inserted into the cell membrane (grey and orange). A representation of the volume accessible to ions is shown in yellow.
Publication : Bioessays

The aminoacyl-tRNA synthetase family: modules at work.

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Bioessays - 01 Oct 1993

Delarue M, Moras D. Bioessays. 1993 Oct;15(10):675-87. Review

Link to Pubmed [PMID] – 8274143

Link to HAL – Click here

Link to DOI – 10.1002/bies.950151007

Bioessays. 1993 Oct;15(10):675-87. Review

The combined use of molecular and structural biology techniques has proved very efficient in elucidating structure-function relationships in aminoacyl-tRNA synthetases. Our present understanding of this family of enzymes is based on two main unifying principles: (i) division into two different classes, corresponding to two different modes of ATP binding and attachment of the activated amino acid to the last nucleotide of tRNA (either 2’OH or 3’OH of the ribose) by two different catalytic mechanisms and two structural domains with completely different folding, and (ii) the modular organization into separate and additional domains that we are just beginning to understand. Sequence analysis complements very nicely existing structural, biochemical and genetic results and makes them more general, leading to verifiable predictions.