The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:"
L22 is the largest protein contributor to the surface of the polypeptide exit channel, the tunnel through which the polypeptide product passes. It is the only ribosomal protein that interacts with all six domains of 23S rRNA, and is one of the proteins important for directing the proper folding and stabilising the conformation of 23S rRNA. L22 is also one of six proteins located at the putative translocon binding site on the exterior surface of the ribosome. The nascent polypeptide interacts with the beta-hairpin of L22.
The triplet Met82-Lys83-Arg84 deletion in L22 from Escherichia coli gives rise to resistance to erythromycin, an inhibitor of the nascent peptide chain elongation. The mutant beta-hairpin is bent inward the ribosome tunnel modifying the shape of its narrowest part and affecting the interaction between L22 and 23 S rRNA. 23 S rRNA nucleotides of domain V participating in erythromycin binding are located on the opposite sides of the tunnel and are brought to those positions by the interaction of the 23 S rRNA with the L22 beta-hairpin. The mutation in the L22 beta-hairpin affects the orientation and distances between those nucleotides. This destabilises the erythromycin-binding "pocket" formed by 23 S rRNA nucleotides exposed at the tunnel surface. It seems that erythromycin, while still being able to interact with one side of the tunnel but not reaching the other, is therefore unable to block the polypeptide growth in the drug-resistant ribosome.
|Domain clusters (>95% seq id):||12|
|Domain clusters (>35% seq id):||6|
|Structural Clusters (5A):||2|
|Structural Clusters (9A):||2|