Sandbox Reserved 814

==Your Heading Here (maybe something like 'Structure')==

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 , a C-terminal region which contains two small 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. . 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  : Leu25, Val40, Val57 and Ile2. This area is very exposed and separated from the RNA binding site. Role of the L14 subunit By Bonhomme Clémence and Dilda Nathan

spinqualitylabelsall models Structure L14 ribosomal protein(PDB entry 1whi) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

spinqualitylabelsall models Insert caption here Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

This Sandbox is Reserved from 06/12/2018, through 30/06/2019 for use in the course "Structural Biology" taught by Bruno Kieffer at the University of Strasbourg, ESBS. This reservation includes Sandbox Reserved 1480 through Sandbox Reserved 1543.

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