Comparative Study
doi: 10.1038/347249a0.
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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- PMID: 2205803
- DOI: 10.1038/347249a0
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Comparative Study
A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A
Nature.
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Abstract
The three-dimensional crystal structure of seryl-transfer RNA synthetase from Escherichia coli, refined at 2.5 A resolution, is described. It has an N-terminal domain that forms an antiparallel alpha helical coiled-coil, stretching 60 A out into the solvent and stabilized by interhelical hydrophobic interactions and an active-site alpha-beta domain based around a seven-stranded antiparallel beta 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.
Comment in
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Synthetase with a difference.Nature. 1990 Sep 20;347(6290):231. doi: 10.1038/347231a0. Nature. 1990. PMID: 2402295 No abstract available.
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