T.M. Schmeing1, Rebecca M. Voorhees1, A.C. Kelley1, Yong‐Gui Gao1, F.V. Murphy1, John R. Weir1, V. Ramakrishnan1
1MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK
Tóm tắt
Ribosomes Caught in Translation
To synthesize proteins, the ribosome must select cognate transfer RNAs (tRNAs) based on base-pairing with the messenger RNA (mRNA) template (a process known as decoding), form a peptide bond, and then move the mRNA:tRNA assembly relative to the ribosome (a process known as translocation). Decoding and translocation require protein guanosine triphosphatases (GTPases), and, while high-resolution structures of the ribosome have greatly furthered our understanding of ribosome function, the detailed mechanism of these GTPases during the elongation cycle remains unclear. Two Research Articles now give a clearer view of these steps in bacterial protein synthesis (see the Perspective by
Liljas
).
Schmeing
et al.
(p.
688
, published online 15 October) present the crystal structure of the ribosome bound to Elongation factor-Tu (EF-Tu) and amino-acyl tRNA that gives insight into how EF-Tu contributes to accurate decoding.
Gao
et al.
(p.
694
, published online 15 October) describe the crystal structure of the ribosome bound to Elongation factor-G (EF-G) trapped in a posttranslocation state by the antibiotic fusidic acid that gives insight into how EF-G functions in translocation.
