In the process of translocation, ribosome keeps on moving from one end of to other end by the distance of one triplet codon. A B C D (A) DNA (B) rRNA (C) tRNA (D) mRNA
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Structures of the ribosomal large and small subunits have been solved to atomic resolution by X-ray crystallography. These structures provide a new foundation to address the complex process of protein biosynthesis by the ribosome. Translocation of the tRNA–mRNA complex is one of the most fascinating tasks performed by the ribosome. The impact of the crystal structures in understanding the molecular mechanism of translocation is highlighted in this review.
As recently as the mid-1990s, obtaining high-resolution structure of the ribosome was considered to be an impossible dream. Today, it is feasible for anybody with a personal computer to download and view atomic resolution structures of both ribosomal subunits (Ban et al. 2000; Schluenzen et al. 2000, 2001; Wimberly et al. 2000). Additionally, structures of the complete ribosome incorporating tRNA and mRNA have been solved at 5.5-Å resolution (Yusupov et al. 2001). This amazing change of events has provided a much-needed structural framework and has revolutionized the field. The remaining challenge is to understand the functional significance of the ribosome structure. One of the most remarkable events during the elongation phase of protein synthesis is the iterative movement of the tRNAs and the associated mRNA through the ribosome. The molecular basis for translocation and mRNA-reading-frame maintenance are largely unknown. Translocation is catalyzed by an elongation factor (EF-G in Escherichia coli) and involves precise and coordinated movement of large molecules (mRNA and two tRNAs) over long distances (∼50 Å) in the ribosome. Furthermore, the ribosome is a dynamic machine that undergoes dramatic conformational changes during translocation. Therefore, in this post-crystal-structure era, the most interesting challenge for ribosome research is to uncover the mechanism of translocation.