Ontology highlight
ABSTRACT:
SUBMITTER: Neubauer C
PROVIDER: S-EPMC3763467 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Neubauer Cajetan C Gillet Reynald R Kelley Ann C AC Ramakrishnan V V
Science (New York, N.Y.) 20120301 6074
In bacteria, ribosomes stalled at the end of truncated messages are rescued by transfer-messenger RNA (tmRNA), a bifunctional molecule that acts as both a transfer RNA (tRNA) and a messenger RNA (mRNA), and SmpB, a small protein that works in concert with tmRNA. Here, we present the crystal structure of a tmRNA fragment, SmpB and elongation factor Tu bound to the ribosome at 3.2 angstroms resolution. The structure shows how SmpB plays the role of both the anticodon loop of tRNA and portions of m ...[more]