Journal
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY
Volume 62, Issue -, Pages 1510-1519Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S0907444906039850
Keywords
-
Ask authors/readers for more resources
Eukaryotic aminoacyl-tRNA synthetases (aaRS) frequently contain additional appended domains that are absent from their prokaryotic counterparts which mediate complex formation between eukaryotic aaRS and cofactors of amino-acylation and translation. However, the structural basis of such interactions has remained elusive. The heteromerization domain of yeast glutamyl-tRNA synthetase (GluRS) has been cloned, expressed, purified and crystallized in space group C2221, with unit-cell parameters a = 52, b = 107, c = 168 angstrom. Phase information was obtained from multiple-wavelength anomalous dispersion with selenomethionine to 2.5 angstrom resolution and the structure, comprising two monomers per asymmetric unit, was determined and refined to 1.9 angstrom resolution. The structure of the interacting domain of its accessory protein Arc1p was determined and refined to 1.9 A resolution in a crystal form containing 20 monomers organized in five tetramers per asymmetric unit (space group C2, unit-cell parameters a = 222, b = 89, c = 127 angstrom, beta = 99.4 degrees). Both domains adopt a GST- like fold, demonstrating a novel role for this fold as a protein - protein interaction module.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available