Structural highlights
Function
[SSRP_THET8] Binds specifically to the SsrA RNA (tmRNA) and is required for stable association of SsrA with ribosomes (By similarity).
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
Small protein B (SmpB) is required for trans-translation, binding specifically to tmRNA. We show here the solution structure of SmpB from an extremely thermophilic bacterium, Thermus thermophilus HB8, determined by heteronuclear nuclear magnetic resonance methods. The core of the protein consists of an antiparallel beta-barrel twisted up from eight beta-strands, each end of which is capped with the second or third helix, and the first helix is located beside the barrel. Its C-terminal sequence (20 residues), which is rich in basic residues, shows a poorly structured form, as often seen in isolated ribosomal proteins. The results are discussed in relation to the oligonucleotide binding fold.
Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus.,Someya T, Nameki N, Hosoi H, Suzuki S, Hatanaka H, Fujii M, Terada T, Shirouzu M, Inoue Y, Shibata T, Kuramitsu S, Yokoyama S, Kawai G FEBS Lett. 2003 Jan 30;535(1-3):94-100. PMID:12560085[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Someya T, Nameki N, Hosoi H, Suzuki S, Hatanaka H, Fujii M, Terada T, Shirouzu M, Inoue Y, Shibata T, Kuramitsu S, Yokoyama S, Kawai G. Solution structure of a tmRNA-binding protein, SmpB, from Thermus thermophilus. FEBS Lett. 2003 Jan 30;535(1-3):94-100. PMID:12560085
