title: Ribosomal proteins and elongation factors.
abstract: Structural work on the translation machinery has recently undergone rapid progress. It is now known that six out of nine ribosomal proteins have an RNA-binding fold, and two domains of elongation factors Tu and G have very similar folds. In addition, the complex of EF-Tu with a GTP analogue and Phe-tRNA(Phe) has a structure that overlaps exceedingly well with that of EF-G-GDP. These findings obviously have functional implications.
authors: University of Lund, Sweden.
authors: A
authors: A
authors: Liljas
authors: M
authors: M
authors: Garber
mesh_terms: D005656:Fungal Proteins; D006153:Guanosine Diphosphate / Q000378:metabolism; D008958:Models, Molecular; D020653:Peptide Elongation Factor G; D010444:Peptide Elongation Factor Tu / Q000737:chemistry / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000737:chemistry* / Q000378:metabolism; D014176:Protein Biosynthesis; D011487:Protein Conformation; D012335:RNA, Ribosomal / Q000737:chemistry; D012269:Ribosomal Proteins / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000648:ultrastructure; D029701:Saccharomyces cerevisiae Proteins
chemical_list: D005656:Fungal Proteins; D020653:Peptide Elongation Factor G; D010445:Peptide Elongation Factors; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; C111584:YEF3 protein, S cerevisiae; D006153:Guanosine Diphosphate; D010444:Peptide Elongation Factor Tu