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:"
L11 consists of a 23S rRNA binding C-terminal domain and an N-terminal domain that directly contacts protein synthesis factors. These two domains are joined by a flexible linker that allows inter-domain movement during protein synthesis. This entry represents the N-terminal domain of L11/L12. The structure of the L11 N-terminal domain (NTD) consists of two helices packed against the concave surface of a three-stranded antiparallel beta sheet, with the first seven residues disordered. One of the most distinctive and conserved regions of the L11 molecule is the proline-rich helix 1, which appears to have a crucial functional role.
L11 is known to bind directly to the 23S rRNA and plays a significant role during initiation, elongation, and termination of protein synthesis. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The N-terminal domain functions as a molecular switch, either by facilitating changes in the tertiary structure of the GAR/GAC (GTPase-associated region/centre) RNA or by controlling access to the RNA. In bacteria, the L11 N-terminal domain is post-translationally modified (trimethylated) at multiple residues by the S-adenosyl-L-methionine(AdoMet)-dependent trimethyltransferase PrmA.
|Domain clusters (>95% seq id):||7|
|Domain clusters (>35% seq id):||3|
|Structural Clusters (5A):||1|
|Structural Clusters (9A):||1|