High-resolution Structures of Ribosomal Subunits: Initiation, Inhibition, and Conformational Variability

The recent impressive progress in ribosomal crystallography has yielded insights into the mechanism ofprotein biosynthesis. Analysis of the high-resolutionstructures (Ban et al. 2000; Schluenzen et al. 2000;Wimberly et al. 2000) has led to the identification ofdynamic aspects of this process and highlighted strategiesadopted by the ribosomes for maintaining their structuralintegrity and for their survival under extreme conditions(Gluehmann et al. 2001; Harms et al. 2001). Naturally,the crystallographic studies have expanded far beyondthe presentation of still pictures and are rapidly progressing toward the elucidation of snapshots describing specific functional stages during the biosynthetic process.Structures of complexes with analogs of transfer RNAand messenger RNA (Weinstein et al. 1999; Auerbach etal. 2000; Brodersen et al. 2000; Yusupov et al. 2001),compounds believed to be substrate analogs (Nissen et al.2000), translation initiation factors (Carter et al. 2001; Pioletti et al. 2001), and antibiotics (Brodersen et al. 2000;Carter et al. 2000; Pioletti et al. 2001; Schlunzen et al.2001) are rapidly emerging...