Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

By A. Carter, W. M. Clemons, D. Brodersen, Robert J. Morgan-Warren, B. Wimberly, V. Ramakrishnan. Nature, 2000

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Selection of tRNA by the ribosome requires a transition from an open to a closed form. (2002, background): “The movement of the spur occurs in these crystals are nearly identical to that of the cognate ASL (Figure because it mimics P site tRNA in a neighboring 30S molecule (Carter et al., 2000 ).”
The non-Watson-Crick base pairs and their associated isostericity matrices. (2002, background): “thermophilus (47) RR0033 50S ribosomal subunit from H.”
Tetracycline Antibiotics and Resistance. (2016, background): “thermophilus crystal structure, these S10 residues map to a loop projecting toward the aminoacyl-tRNA-binding site in the 30S structure (Brodersen et al. 2000; Carter et al. 2000).”
The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. (2000, background): “The increase in the chemical reactivity of N1of A1408, which is about the tRNA anticodon stem loop relative to the codon:anti-codon interaction (Figure 2b) (Carter et al., 2000).”