PMID:2205803

Citation	Cusack, S, Berthet-Colominas, C, Härtlein, M, Nassar, N and Leberman, R (1990) A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature 347:249-55
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.
Links	PubMed Online version:10.1038/347249a0
Keywords	Amino Acid Sequence; Amino Acyl-tRNA Synthetases; Binding Sites; Crystallization; Escherichia coli/enzymology; Macromolecular Substances; Molecular Sequence Data; Molecular Structure; Protein Conformation; Sequence Homology, Nucleic Acid; Serine-tRNA Ligase; X-Ray Diffraction
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