spacer
spacer

Jump to: InterProScan Databases Documentation FTP site Help Advanced search

InterPro: IPR001787 Ribosomal protein L21

Protein matchesHelp
UniProtKB
Matches:
1828 proteins
AccessionHelp IPR001787 Ribosomal_L21
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR018258 Ribosomal protein L21, conserved site
GO Term annotationHelp
Process GO:0006412 translation
Function GO:0003723 RNA binding
GO:0003735 structural constituent of ribosome
Component GO:0005622 intracellular
GO:0005840 ribosome
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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 [1, 2]. 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 of 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 [2, 3].

Ribosomal protein L21 is one of the proteins from the large ribosomal subunit. In Escherichia coli, L21 is known to bind to the 23S rRNA in the presence of L20. It belongs to a family of ribosomal proteins which, on the basis of sequence similarities, groups:

  • Bacterial L21.
  • Marchantia polymorpha chloroplast L21.
  • Cyanelle L21.
  • Plant chloroplast L21 (nuclear-encoded).

Bacterial L21 is a protein of about 100 amino-acid residues, the mature form of the spinach chloroplast L21 has 200 residues.

Structural linksHelp
PDB - click here
Database linksHelp
PDBe-motif: PS01169
PROSITE doc: PDOC00899
PANDIT: PF00829
Blocks: IPB001787

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001787 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P40858 54S ribosomal protein L49, mitochondrial

P51412 50S ribosomal protein L21, chloroplastic

P74266 50S ribosomal protein L21

Q7Z2W9 39S ribosomal protein L21, mitochondrial

Q9D1N9 39S ribosomal protein L21, mitochondrial

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR015934 Aconitase/Iron regulatory protein 2/2-methylisocitrate dehydratase
IPR001787 Ribosomal protein L21
IPR018258 Ribosomal protein L21, conserved site
IPR015937 Aconitase-like core
SWISS-MODEL
ModBase

PublicationsHelp
1. Ramakrishnan V, Moore PB.
Atomic structures at last: the ribosome in 2000.
Curr. Opin. Struct. Biol. 11 144-54 2001 [PubMed: 11297922]
http://dx.doi.org/10.1016/S0959-440X(00)00184-6
2. Maguire BA, Zimmermann RA.
The ribosome in focus.
Cell 104 813-6 2001 [PubMed: 11290319]
http://dx.doi.org/10.1016/S0092-8674(01)00278-1
3. Chandra Sanyal S, Liljas A.
The end of the beginning: structural studies of ribosomal proteins.
Curr. Opin. Struct. Biol. 10 633-6 2000 [PubMed: 11114498]
http://dx.doi.org/10.1016/S0959-440X(00)00143-3

Additional ReadingHelp
Laurberg M, Asahara H, Korostelev A, Zhu J, Trakhanov S, Noller HF.
Structural basis for translation termination on the 70S ribosome.
Nature 454 2008 852-7 [PubMed: 18596689]
http://dx.doi.org/10.1038/nature07115
Harms JM, Wilson DN, Schluenzen F, Connell SR, Stachelhaus T, Zaborowska Z, Spahn CM, Fucini P.
Translational regulation via L11: molecular switches on the ribosome turned on and off by thiostrepton and micrococcin.
Mol. Cell 30 2008 26-38 [PubMed: 18406324]
http://dx.doi.org/10.1016/j.molcel.2008.01.009
Borovinskaya MA, Shoji S, Fredrick K, Cate JH.
Structural basis for hygromycin B inhibition of protein biosynthesis.
RNA 14 2008 1590-9 [PubMed: 18567815]
http://dx.doi.org/10.1261/rna.1076908
Bingel-Erlenmeyer R, Kohler R, Kramer G, Sandikci A, Antolic S, Maier T, Schaffitzel C, Wiedmann B, Bukau B, Ban N.
A peptide deformylase-ribosome complex reveals mechanism of nascent chain processing.
Nature 452 2008 108-11 [PubMed: 18288106]
http://dx.doi.org/10.1038/nature06683
Wilson DN, Schluenzen F, Harms JM, Starosta AL, Connell SR, Fucini P.
The oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning.
Proc. Natl. Acad. Sci. U.S.A. 105 2008 13339-44 [PubMed: 18757750]
http://dx.doi.org/10.1073/pnas.0804276105
spacer
spacer
InterPro 23.1