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The 30S ribosomal subunit is responsible for binding mRNA and the anticodon stem loop of tRNA. By monitoring codon-anticodon interactions in the decoding process, it greatly increases the fidelity of translation. Although the smaller of the two subunits, it has a molecular weight of almost a megadalton, and determination of its structure presented challenging problems in crystallization, data collection and phasing. We describe some general conclusions from the structure determination of the 30S ribosomal subunit. In particular, careful and extensive use of anomalous scattering was essential to obtaining useful high resolution phases. We also describe insights into the decoding mechanism from the structure of the 30S subunit complexed with antibiotics and mRNA and tRNA ligands. The 30S subunit discriminates between correct and incorrect tRNAs through an induced fit mechanism that closely monitors the minor groove geometry of base pairing at the first two positions of the codon-anticodon helix. These studies provide a structural rationale for the wobble hypothesis and why degeneracy in the genetic code is tolerated at the third position. They also show in structural terms how aminoglycoside antibiotics affect the fidelity of translation.

Crystallographic lessons and functional insights from the structure of the 30S subunit