title: After the ribosome structure: how does translocation work?
abstract: Structures of the ribosomal large and small subunits have been solved to atomic resolution by X-ray crystallography. These structures provide a new foundation to address the complex process of protein biosynthesis by the ribosome. Translocation of the tRNA-mRNA complex is one of the most fascinating tasks performed by the ribosome. The impact of the crystal structures in understanding the molecular mechanism of translocation is highlighted in this review.
authors.affiliation: Department of Chemistry and Biochemistry, University of California-San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0314, USA. sjoseph@chem.ucsd.edu
authors.forename: Simpson
authors.initials: S
authors.lastname: Joseph
mesh_terms: D001419:Bacteria / Q000737:chemistry / Q000378:metabolism; D020653:Peptide Elongation Factor G / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012343:RNA, Transfer / Q000378:metabolism*; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D020653:Peptide Elongation Factor G; D012333:RNA, Messenger; D012343:RNA, Transfer