Structural highlights
Function
[RL18_BACST] This is one of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance.
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
A medium resolution solution structure has been obtained for L18 from Bacillus stearothermophilus (BstL18), a ribosomal protein that stabilizes the tertiary structure of 5S rRNA and mediates its interaction with the rest of the large subunit. The N-terminal 22 amino acid residues of BstL18 are unstructured in solution. Its remaining 98 residues form a globular domain that has the same topology as the globular domains of other L18s, but the orientation of helices is different. This conformational peculiarity should not prevent BstL18 from functioning in the ribosome the same way as other L18s.
The solution structure of ribosomal protein L18 from Bacillus stearothermophilus.,Turner CF, Moore PB J Mol Biol. 2004 Jan 16;335(3):679-84. PMID:14687565[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Turner CF, Moore PB. The solution structure of ribosomal protein L18 from Bacillus stearothermophilus. J Mol Biol. 2004 Jan 16;335(3):679-84. PMID:14687565
