The ribosome revealed Trends in Biochemical Sciences Peter B. Moore, Thomas A. Steitz  Trends in Biochemical Sciences  Volume 30, Issue 6, Pages 281-283 (June 2005) DOI: 10.1016/j.tibs.2005.04.006 Copyright © 2005 Elsevier Ltd Terms and Conditions

Figure 1 A space-filling model of the 70S ribosome generated using the structures of the Haloarcula marismortui large subunit [3] and the Thermus thermophilus small subunit [4] docked by superposition on the rRNA model for the T. thermophilus 70S ribosomes [20] in addition to the A-, P- and E-site tRNAs from that model. 23S rRNA and 5S rRNA are purple and white; the 16S rRNA is yellow. Ribosomal proteins of the large subunit are blue and those of the small subunit are green. The A-site tRNA with its 3′ end extending into the peptidyl-transferase cavity is red and the P-site tRNA is yellow. Reproduced, with permission, from Ref. [21]. Trends in Biochemical Sciences 2005 30, 281-283DOI: (10.1016/j.tibs.2005.04.006) Copyright © 2005 Elsevier Ltd Terms and Conditions

Figure 2 Superposition of the structures of several antibiotics bound to the large ribosomal subunit from Haloarcula marismortui. The large subunit has been sliced open to reveal its peptidyl-transferase region, which is shown as a gray solvent contact surface, and an A-site substrate, CCA-puromycin (red), and a P-site substrate, CCA-phenylalanine-caproic acid-biotin (orange), are shown. The positions occupied by six antibiotics are displayed: sparsomycin (green), puromycin (red), blasticidin (purple), streptogramin A (cyan), carbomycin, which is a macrolide, (blue), and chloramphenicol (light blue). Reproduced, with permission, from Ref. [17]. Trends in Biochemical Sciences 2005 30, 281-283DOI: (10.1016/j.tibs.2005.04.006) Copyright © 2005 Elsevier Ltd Terms and Conditions