G3DSA:2.30.30.770

G3DSA:2.30.30.770

CATH-Gene3D entry
Member databaseCATH-Gene3D
CATH-Gene3D typehomologous superfamily

Description
Imported from IPR038655

This entry represents the large ribosomal subunit protein eL27 (also known as L27) found in fungi, plants, algae and vertebrates
[3, 2]
.

Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites
[5, 4]
. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits.

Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome
[4, 1]
.

References
Imported from IPR038655

1.The end of the beginning: structural studies of ribosomal proteins. Chandra Sanyal S, Liljas A. Curr. Opin. Struct. Biol. 10, 633-6, (2000). View articlePMID: 11114498

2.Nucleotide sequence of a cDNA clone for a 60S ribosomal protein L27 gene from potato (Solanum tuberosum L.). Taylor MA, Davies HV. Plant Physiol. 105, 1025-6, (1994). View articlePMID: 8058833

3.Cloning and nucleotide sequence of a full length cDNA encoding ribosomal protein L27 from human fetal kidney. Gallagher RA, McClean PM, Malik AN. Biochim. Biophys. Acta 1217, 329-32, (1994). View articlePMID: 8148381

4.The ribosome in focus. Maguire BA, Zimmermann RA. Cell 104, 813-6, (2001). View articlePMID: 11290319

5.Atomic structures at last: the ribosome in 2000. Ramakrishnan V, Moore PB. Curr. Opin. Struct. Biol. 11, 144-54, (2001). View articlePMID: 11297922

This website requires cookies, and the limited processing of your personal data in order to function. By using the site you are agreeing to this as outlined in our Privacy Notice and Terms of Use.