TY - JOUR
AU1 - Cusack, Stephen
AU2 - Berthet-Colominas, Carmen
AU3 - Härtlein, Michael
AU4 - Nassar, Nicolas
AU5 - Leberman, Reuben
AB - 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.
TI - A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 Å
JF - Nature
DO - 10.1038/347249a0
DA - 1990-09-20
UR - https://www.deepdyve.com/lp/springer-journals/a-second-class-of-synthetase-structure-revealed-by-x-ray-analysis-of-90ISSsLrPY
SP - 249
EP - 255
VL - 347
IS - 6290
DP - DeepDyve
ER -