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 |
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Hauptverfasser: | , , , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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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. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/347249a0 |