title: Elongation in bacterial protein biosynthesis.
abstract: The past year has brought some notable advances in our understanding of the structure and function of elongation factors (EFs) involved in protein biosynthesis. The structures of the ternary complex of aminoacylated tRNA with EF-Tu.GTP and of the complex EF-Tu.EF-Ts have been determined. Within the same period, new cryo-electron microscopy reconstructions of ribosome particles have been obtained.
authors.affiliation: Department of Molecular and Structural Biology, University of Aarhus, Denmark. jnb@kemi.aau.dk
authors.forename: J
authors.initials: J
authors.lastname: Nyborg
authors.forename: M
authors.initials: M
authors.lastname: Kjeldgaard
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis*; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D008954:Models, Biological; D008958:Models, Molecular; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D012270:Ribosomes / Q000737:chemistry / Q000648:ultrastructure
chemical_list: D001426:Bacterial Proteins; D010445:Peptide Elongation Factors; C023512:elongation factor Ts; D006160:Guanosine Triphosphate; D010444:Peptide Elongation Factor Tu