Structural highlights
Function
[RF3_DESVM] Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP (By similarity).
Publication Abstract from PubMed
The bacterial translational GTPases release factor RF3 promotes translation termination by recycling RF1 or RF2. Here, we present the crystal structures of RF3 complexed with GDP and guanosine 3',5'-(bis)diphosphate (ppGpp) at resolutions of 1.8 and 3.0A, respectively. ppGpp is involved in the so-called "stringent response" of bacteria. ppGpp binds at the same site as GDP, suggesting that GDP and ppGpp are two alternative physiologically relevant ligands of RF3. We also found that ppGpp decelerates the recycling of RF1 by RF3. These lines of evidence suggest that RF3 functions both as a cellular metabolic sensor and as a regulator.
Crystal structure analysis of the translation factor RF3 (release factor 3).,Kihira K, Shimizu Y, Shomura Y, Shibata N, Kitamura M, Nakagawa A, Ueda T, Ochi K, Higuchi Y FEBS Lett. 2012 Oct 19;586(20):3705-9. doi: 10.1016/j.febslet.2012.08.029. Epub, 2012 Sep 6. PMID:22975312[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kihira K, Shimizu Y, Shomura Y, Shibata N, Kitamura M, Nakagawa A, Ueda T, Ochi K, Higuchi Y. Crystal structure analysis of the translation factor RF3 (release factor 3). FEBS Lett. 2012 Oct 19;586(20):3705-9. doi: 10.1016/j.febslet.2012.08.029. Epub, 2012 Sep 6. PMID:22975312 doi:10.1016/j.febslet.2012.08.029
