IQUIFIB   02644
INSTITUTO DE QUIMICA Y FISICOQUIMICA BIOLOGICAS "PROF. ALEJANDRO C. PALADINI"
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
Structure-Function relationship of the Sterol Carrier Protein from the yeast Yarrowia lipolytica (YLSCP2)
Autor/es:
NOELIA I. BURGARDT; FEDERICO J. PÉREZ DE BERTI; RAÚL G. FERREYRA; CHRISTIAN LÜCKE; BETINA CORSICO; MARIO R. ERMÁCORA; MARCELO R. CEOLÍN
Lugar:
Frankfurt am Main
Reunión:
Congreso; EUROMAR; 2011
Resumen:
The sterol carrier proteins (SCP2) are small soluble intracellular proteins highly conserved in all biological kingdoms. The SCP2 spectrum of ligands is broad, including fatty acids, acyl-CoAs, sterols and phospholipids. The L-shaped ligand binding site shows a high conformational plasticity, which could be related to the binding mechanism 1. Our aim is to study the structure-function relationship of YLSCP2, a yeast member of the sterol carrier protein family 2.The effect of ligand binding on the structure and stability of the protein was evaluated by several techniques (CD, fluorescence, SAXS, and thermal unfolding). The stability of YLSCP2 decreases after cis-parinaric acid and ANS binding. The secondary structure content of YSCP2 decreases with palmitic acid and cholesterol binding. The intrinsic fluorescence decreases with palmitoyl-CoA.The differential effects of ligand binding on YLSCP2 structure and stability could be correlated with the conformational plasticity of the binding site. To elucidate the ligand binding mechanism we are planning to perform NMR experiments, in order to identify the residues that define the binding site for each ligand.REFERENCES:1. Filipp F. V., Sattler M., Biochemistry, 46, 7980-91 (2007)2. Ferreyra R. G., et al, Arch. Biochem. Biophys., 453, 197-206 (2006)