Structural highlights
Function
RS18_THET8 Located on the back of the platform of the 30S subunit where it stabilizes the close packing of several RNA helices of the 16S rRNA. Forms part of the Shine-Dalgarno cleft in the 70S ribosome, where it probably interacts with the Shine-Dalgarno helix.[HAMAP-Rule:MF_00270]
Publication Abstract from PubMed
A key step of translation by the ribosome is translocation, which involves the movement of messenger RNA (mRNA) and transfer RNA (tRNA) with respect to the ribosome. This allows a new round of protein chain elongation by placing the next mRNA codon in the A site of the 30S subunit. Translocation proceeds through an intermediate state in which the acceptor ends of the tRNAs have moved with respect to the 50S subunit but not the 30S subunit, to form hybrid states. The guanosine triphosphatase (GTPase) elongation factor G (EF-G) catalyzes the subsequent movement of mRNA and tRNA with respect to the 30S subunit. Here, we present a crystal structure at 3 angstrom resolution of the Thermus thermophilus ribosome with a tRNA in the hybrid P/E state bound to EF-G with a GTP analog. The structure provides insights into structural changes that facilitate translocation and suggests a common GTPase mechanism for EF-G and elongation factor Tu.
Elongation factor G bound to the ribosome in an intermediate state of translocation.,Tourigny DS, Fernandez IS, Kelley AC, Ramakrishnan V Science. 2013 Jun 28;340(6140):1235490. doi: 10.1126/science.1235490. PMID:23812720[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Tourigny DS, Fernandez IS, Kelley AC, Ramakrishnan V. Elongation factor G bound to the ribosome in an intermediate state of translocation. Science. 2013 Jun 28;340(6140):1235490. doi: 10.1126/science.1235490. PMID:23812720 doi:10.1126/science.1235490
