A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
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.
Grenoble Outstation, European Molecular Biology Laboratory, France.
S
S
Cusack
C
C
Berthet-Colominas
M
M
Härtlein
N
N
Nassar
R
R
Leberman
D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases; D001665:Binding Sites; D003460:Crystallization; D004926:Escherichia coli / Q000201:enzymology*; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011487:Protein Conformation; D012689:Sequence Homology, Nucleic Acid; D012714:Serine-tRNA Ligase; D014961:X-Ray Diffraction
D046911:Macromolecular Substances; D000604:Amino Acyl-tRNA Synthetases; D012714:Serine-tRNA Ligase