Sandbox Reserved 814: Difference between revisions

The L14 subunit has a molecular mass of 13.3 kDa and contains 122 amino acids. The molecule is extremly compact so water molecule are exclude. It belong to α+β class of proteins. It is composed of five stranded <scene name='56/568012/Barrel/1'>beta barrel</scene> : β1-β2-β3-β4-β7 all antiparallel, stabilized by hydrogen-bounding, a C-terminal region which contains the two small <scene name='56/568012/Helix/2'>alpha-helixes</scene> and a beta-ribbon : the extended loop8. The beta-barrel contains a hydrophobic core of highly conserved residues : Ala, Leu, Ile, Val, Cys. The beta-barrel is stabilized by some hydrogen-bonding such as a bonding between loop 2 and loops 4 and 8. <scene name='56/568012/Loopstab/1'>Loop 4 interact with the Ser14 of the loop 2 by the residue 51</scene>. The loops 3 which connects β2 and β3 allows to close this end with the hydrophobic side chains. The top of the β-barrel is doing by 2 valines 51 and 54 in loop 4

The loop 2 have an unusual and highly structure turn which contains the most conserved sequence, stabilized by a complexe hydrogen-bonding : the alide protons and carbonyl oxygène of 3 residues and a water molecule. The turn allow to stabilize loop 4 and loop 8. Loop8 has several interactions. Finally, three structural waters (206–208) are involved in stabilizing the local conformation around residue 91 in loop8 and the N terminus of helix α2.