Sandbox Reserved 814: Difference between revisions
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== Structure == | == Structure == | ||
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 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 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 made with 2 valines 51 and 54 in loop 4. | ||
The loop 2 has an unusual and highly structure turn which contains the most conserved sequence, stabilized by a hydrogen-bonding complex: the alide protons and carbonyl oxygène of 3 residues and a water molecule. The turn allows to stabilize loop 4 and loop 8. Loop8 has several interactions. Finally, three structural waters (206–208) are involved in the stabilization of the local conformation around residue 91 in loop8 and the N terminus of helix α2. | |||
== Bidding sites == | == Bidding sites == | ||
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Christopher Davies, Stephen W White, V Ramakrishnan. The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus. | Christopher Davies, Stephen W White, V Ramakrishnan. The crystal structure of ribosomal protein L14 reveals an important organizational component of the translational apparatus. | ||
L. Mattheakis, L. Vu, F. Sor, M. Nomura ; Octobre 1988. Retroregulation of the synthesis of ribosomal protein L14 and L24 by feedback repressor S8 in Escherichia coli.. | |||
By Bonhomme Clémence and Dilda Nathan</StructureSection><!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | By Bonhomme Clémence and Dilda Nathan</StructureSection><!-- PLEASE DO NOT DELETE THIS TEMPLATE --> | ||
{{Sandbox_Reserved_ESBS}} | {{Sandbox_Reserved_ESBS}} | ||
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