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

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 in...

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Veröffentlicht in:Nature (London) 1990-09, Vol.347 (6290), p.249-255
Hauptverfasser: Cusack, Stephen, Berthet-Colominas, Carmen, Härtlein, Michael, Nassar, Nicolas, Leberman, Reuben
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Sprache:eng
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Zusammenfassung: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.
ISSN:0028-0836
1476-4687
DOI:10.1038/347249a0