Structural highlights
Function
[RL11_BACST] Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
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
The X-ray crystal structure of a ribosomal L11-rRNA complex with chloroplast-like mutations in both protein and rRNA is presented. The global structure is almost identical to that of the wild-type (bacterial) complex, with only a small movement of the protein alpha helix away from the surface of the RNA required to accommodate the altered protein residue. In contrast, the specific hydrogen bonding pattern of the mutated residues is substantially different, and now includes a direct interaction between the protein side chain and an RNA base edge and a water-mediated contact. Comparison of the two structures allows the observations of sequence variation and relative affinities of wild-type and mutant complexes to be clearly rationalized, but reinforces the concept that there is no single simple code for protein-RNA recognition.
Coevolution of protein and RNA structures within a highly conserved ribosomal domain.,Dunstan MS, Guhathakurta D, Draper DE, Conn GL Chem Biol. 2005 Feb;12(2):201-6. PMID:15734647[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dunstan MS, Guhathakurta D, Draper DE, Conn GL. Coevolution of protein and RNA structures within a highly conserved ribosomal domain. Chem Biol. 2005 Feb;12(2):201-6. PMID:15734647 doi:10.1016/j.chembiol.2004.11.019
