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

Nature volume 347, pages 249–255 (1990) Cite this article

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Abstract

The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 Å resolution, is described. It has an N-terminal domain that forms an antiparallel α helical coiled-coil, stretching 60 Å out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site α – β domain based around a seven-stranded antiparallel β sheet. Unlike the three other known synthetase structures, the enzyme contains no classical nucleotide-binding fold, and is the first representative of a second class of aminoacyl-tRNA synthetase structures.

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Authors and Affiliations

  1. Grenoble Outstation, European Molecular Biology Laboratory, c/o ILL, 156X, 38042, Grenoble Cedex, France

    Stephen Cusack, Carmen Berthet-Colominas, Michael Härtlein, Nicolas Nassar & Reuben Leberman

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  1. Stephen Cusack
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  2. Carmen Berthet-Colominas
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  3. Michael Härtlein
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  4. Nicolas Nassar
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  5. Reuben Leberman
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Cusack, S., Berthet-Colominas, C., Härtlein, M. et al. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å. Nature 347, 249–255 (1990). https://doi.org/10.1038/347249a0

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