Structural highlights
Function
[RRF_THEMA] Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Ribosome recycling factor (RRF), together with elongation factor G (EF-G), catalyzes recycling of ribosomes after one round of protein synthesis. The crystal structure of RRF was determined at 2.55 angstrom resolution. The protein has an unusual fold where domain I is a long three-helix bundle and domain II is a three-layer beta/alpha/beta sandwich. The molecule superimposes almost perfectly with a transfer RNA (tRNA) except that the amino acid-binding 3' end is missing. The mimicry suggests that RRF interacts with the posttermination ribosomal complex in a similar manner to a tRNA, leading to disassembly of the complex. The structural arrangement of this mimicry is entirely different from that of other cases of less pronounced mimicry of tRNA so far described.
Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic.,Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A Science. 1999 Dec 17;286(5448):2349-52. PMID:10600747[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Selmer M, Al-Karadaghi S, Hirokawa G, Kaji A, Liljas A. Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science. 1999 Dec 17;286(5448):2349-52. PMID:10600747
