A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
Cusack, S., Berthet-Colominas, C., Hartlein, M., Nassar, N., Leberman, R.(1990) Nature 347: 249-255
- PubMed: 2205803 
- DOI: https://doi.org/10.1038/347249a0
- Primary Citation of Related Structures:  
9QMP - PubMed 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.
Organizational Affiliation: 
Grenoble Outstation, European Molecular Biology Laboratory, France.