title: Solution structure of the 162 residue C-terminal domain of human elongation factor 1Bgamma.
abstract: The multisubunit elongation factor 1 (eEF1) is required for the elongation step of eukaryotic protein synthesis. The eEF1 complex consists of four subunits: eEF1A, a G-protein that shuttles aminoacylated tRNAs to the ribosome; eEF1Balpha and eEF1Bbeta, two guanine nucleotide exchange factors, and eEF1Bgamma. Although its exact function remains unknown, this latter subunit is present in all eukaryotes. Recombinant human eEF1Bgamma has been purified and shown to consist of two independent domains. We have utilized high resolution NMR to determine the three-dimensional structure of the 19 kDa C-terminal fragment (domain 2). The structure consists of a five-stranded anti-parallel beta-sheet surrounded by alpha-helices and resembles a contact lens. Highly conserved residues are mainly located on the concave face, suggesting thereby that this side of the molecule might be involved in some biologically relevant interface(s). Although the isolated domain 2 appears to be mostly monomeric in solution, biochemical and structural data indicate a potential homodimer. The proposed dimer model can be further positioned within the quaternary arrangement of the whole eEF1 assembly.
authors.affiliation: Leiden Institute of Chemistry, Gorlaeus Laboratory, University of Leiden, Einsteinweg 55, 2333 CC Leiden, The Netherlands.
authors.forename: Sophie
authors.initials: S
authors.lastname: Vanwetswinkel
authors.forename: Jan
authors.initials: J
authors.lastname: Kriek
authors.forename: Gregers R
authors.initials: GR
authors.lastname: Andersen
authors.forename: Peter
authors.initials: P
authors.lastname: Güntert
authors.forename: Jan
authors.initials: J
authors.lastname: Dijk
authors.forename: Gerard W
authors.initials: GW
authors.lastname: Canters
authors.forename: Gregg
authors.initials: G
authors.lastname: Siegal
mesh_terms: D000595:Amino Acid Sequence; D019992:Databases as Topic; D019281:Dimerization; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020648:Peptide Elongation Factor 1 / Q000737:chemistry*; D010957:Plasmids / Q000378:metabolism; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012313:RNA / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid
chemical_list: D020648:Peptide Elongation Factor 1; D011994:Recombinant Proteins; D012313:RNA