InterPro domain: IPR036769

General Information

  • Identifier IPR036769
  • Description Ribosomal protein L11, C-terminal domain superfamily
  • Number of genes 643
  • Gene duplication stats Loading...

Abstract

Ribosomal protein L11 is one of the proteins from the large ribosomal subunit. In Escherichia coli, L11 is known to bind directly to the 23S rRNA and plays a significant role during initiation, elongation, and termination of protein synthesis. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities [ 1 ], groups bacteria, plant chloroplast, red algal chloroplast, cyanelle and archaeabacterial L11; and mammalian, plant and yeast L12 (YL15). L11 is a protein of 140 to 165 amino-acid residues. 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. 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 [ 2 , 3 , 4 , 5 ]. In E. coli, the C-terminal half of L11 has been shown [ 6 ] to be in an extended and loosely folded conformation and is likely to be buried within the ribosomal structure.

This entry represents the C-terminal domain of L11/L12. The domain consists of a three-helical bundle and a short parallel two-stranded beta-ribbon, with an overall alpha3-beta4-alpha4-alpha5-beta5 topology. All five secondary structure elements contribute to a conserved hydrophobic core. The domain is characterised by two extended loops that are disordered in the absence of the RNA but have defined structures in the complex [ 7 ].


1. The 26S rRNA binding ribosomal protein equivalent to bacterial protein L11 is encoded by unspliced duplicated genes in Saccharomyces cerevisiae. Nucleic Acids Res. 18, 4409-16
2. Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin. Mol. Cell 30, 26-38
3. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell 97, 491-502
4. Recognition of ribosomal protein L11 by the protein trimethyltransferase PrmA. EMBO J. 26, 567-77
5. Multiple-site trimethylation of ribosomal protein L11 by the PrmA methyltransferase. Structure 16, 1059-66
6. Structural properties of ribosomal protein L11 from Escherichia coli. Biochem. Int. 19, 1323-38

Species distribution

Gene table

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