Sandbox Reserved 814: Difference between revisions
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== Introduction == | |||
The L14 ribosomal protein is a protein which is included in the 50S subunit of the procaryote ribosome and in the 60s subunit of the eucaryote ribosome. The 50S and 60S subunits are the twos biggest subunits of the prokaryotic and eukaryotic ribosomes. They participate to the mechanism of translation by allowing the folding and stabilization of rRNA. | |||
The L14 subunit is one of the most conserved protein in the ribosome. L14 has been located at the 50S and 30S subunit interface between peptidyl transferase and GTPase regions. It allows contacts with the 16S rRNA of the 30S subunit (bridges B5 and B8) connecting the 2 subunits. | |||
== Structure == | |||
The L14 subunit has a molecular mass of 13.3 kDa and contains 122 amino acids. It is composed of five stranded beta-barrel, a C-terminal region which contains two small alpha-helixes and a beta-ribbon. The beta-barrel contains a hydrophobic core of highly conserved residues. The beta-barrel is stabilized by some hydrogen-bonding such as a bonding between loop 2 and loops 4 and 8. Loop 4 interact with the Ser14 of the loop 2 by the residue 51. | |||
== Bidding sites == | |||
Protein-protein interactions are essential for the stability of ribosomes. The L14 subunits presents a perfect hydrophobic area on its structure too allow such an interaction with other ribosome’s subunits. This area is on the beta-barrel and is composed of for residues : Leu25, Val40, Val57 and Ile2. This area is very exposed and separated from the RNA binding site. | |||
== | == Role of the L14 subunit == | ||
