InterPro : IPR005880

Name  Ribosomal protein L2, bacterial/organellar-type Short Name  Ribosomal_L2_bac/org-type
Type  Family Description  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 [, ]. 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 [, ].The protein L2 is found in all ribosomes and is one of the best conserved proteins of this mega-dalton complex. L2 is elongated, exposing one end of the protein to the surface of the intersubunit interface of the 50 S subunit and is essential for the association of the ribosomal subunits and might participate in the binding and translocation of the tRNAs []. This entry represents bacterial, chloroplast and mitochondrial forms.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

7 Contains

Id Name Short Name Type
IPR012340 Nucleic acid-binding, OB-fold NA-bd_OB-fold Domain
IPR008991 Translation protein SH3-like domain Translation_prot_SH3-like Domain
IPR022669 Ribosomal protein L2, C-terminal Ribosomal_L2_C Domain
IPR022666 Ribosomal Proteins L2, RNA binding domain Rbsml_prot_L2_RNA-bd_dom Domain
IPR014722 Ribosomal protein L2 domain 2 Rib_L2_dom2 Domain
IPR014726 Ribosomal protein L2, domain 3 Ribosomal_L2_dom3 Domain
IPR022671 Ribosomal protein L2, conserved site Ribosomal_L2_CS Conserved_site

0 Found In

1 Parent Features

Id Name Short Name Type
IPR002171 Ribosomal protein L2 Ribosomal_L2 Family

4 Publications

First Author Title Year Journal Volume Pages
Ramakrishnan V Atomic structures at last: the ribosome in 2000. 2001 Curr Opin Struct Biol 11 144-54
Maguire BA The ribosome in focus. 2001 Cell 104 813-6
Chandra Sanyal S The end of the beginning: structural studies of ribosomal proteins. 2000 Curr Opin Struct Biol 10 633-6
Willumeit R Localization of the protein L2 in the 50 S subunit and the 70 S E. coli ribosome. 2001 J Mol Biol 305 167-77



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)