title: Three-dimensional reconstruction of the valyl-tRNA synthetase/elongation factor-1H complex and localization of the delta subunit.
abstract: Eukaryotic valyl-tRNA synthetase (ValRS) and the heavy form of elongation factor 1 (EF-1H) are isolated as a stable high molecular mass complex that catalyzes consecutive steps in protein biosynthesis--aminoacylation of tRNA and its transfer to elongation factor. Herein is the first three-dimensional structure of the particle as calculated from electron microscopic images of negatively stained samples of the human ValRS/EF-1H complex. The ca. 12 x 8 nm particle has two distinct domains and each appears to have twofold symmetry. Bound antibodies place two delta subunits near the particle's center. These data support a dimeric head-to-head arrangement of particle components.
authors.affiliation: Department of Biochemistry, The University of Mississippi Medical Center, Jackson, MS 39216-4505, USA.
authors.forename: Shoulei
authors.initials: S
authors.lastname: Jiang
authors.forename: Cindy L
authors.initials: CL
authors.lastname: Wolfe
authors.forename: J Anthony
authors.initials: JA
authors.lastname: Warrington
authors.forename: Mona Trempe
authors.initials: MT
authors.lastname: Norcum
mesh_terms: D006801:Humans; D010445:Peptide Elongation Factors / Q000737:chemistry*; D011487:Protein Conformation; D021122:Protein Subunits / Q000737:chemistry; D014637:Valine-tRNA Ligase / Q000737:chemistry*
chemical_list: D010445:Peptide Elongation Factors; D021122:Protein Subunits; C057342:peptide elongation factor 1H; D014637:Valine-tRNA Ligase