The high-resolution structures of ribosomal subunits published in 2000 have revolutionized
the field of protein translation. They facilitated the determination and interpretation of …

GTP-binding (G) proteins constitute a class of P-loop (phosphate-binding loop) proteins that
work as molecular switches between the GDP-bound OFF and the GTP-bound ON state. The …

Peptide-chain elongation during protein synthesis entails sequential aminoacyl-tRNA
selection and translocation reactions that proceed rapidly (2–20 per second) and with a low …

During translation, a conserved GTPase elongation factor—EF-G in bacteria or eEF2 in
eukaryotes—translocates tRNA and mRNA through the ribosome. EF-G has been proposed …

Elongation factor G (EF-G) is a guanosine triphosphatase (GTPase) that plays a crucial role
in the translocation of transfer RNAs (tRNAs) and messenger RNA (mRNA) during …

During protein synthesis, the ribosome controls the movement of tRNA and mRNA by means
of large-scale structural rearrangements. We describe structures of the intact bacterial …

Protein synthesis is one of the major targets in the cell for antibiotics. This review endeavors
to provide a comprehensive “post-ribosome structure” A–Z of the huge diversity of antibiotics …

The elongation cycle of protein synthesis involves the delivery of aminoacyl-transfer RNAs to
the aminoacyl-tRNA-binding site (A site) of the ribosome, followed by peptide-bond …

Ribosomes, which are central to protein synthesis and convert transcribed mRNAs into
polypeptide chains, have been the focus of structural and biochemical studies for more than …

The sequential addition of amino acids to a growing polypeptide chain is carried out by the
ribosome in a complicated multistep process called the elongation cycle. It involves accurate …