TY - JOUR
T1 - NMR studies of the conformation of thiocellobiose bound to a β-glucosidase from Streptomyces sp.
AU - Montero, Esther
AU - Vallmitjana, Miquel
AU - Pérez-Pons, Josep A.
AU - Querol, Enrique
AU - Jiménez-Barbero, Jesús
AU - Cañada, F. Javier
PY - 1998/1/16
Y1 - 1998/1/16
N2 - The conformation of 4-thiocellobiose bound to β-glucosidase from Streptromyces sp. has been studied by 1H-NMR transferred nuclear Overhauser effect spectroscopy (TR-NOE). Thiocellobiose behaves as an inhibitor of this glucosidase when cellobiose is used as substrate. NOE measurements and molecular mechanics calculations have also been performed to estimate the probability distribution of conformers of thiocellobiose when free in solution. Experimental data show that, in contrast with the natural O-analogue, thiocellobiose presents three conformational families in the free state, namely syn, anti-Ψ and anti-Φ whilst only one of them (syn) is recognized by the enzyme.
AB - The conformation of 4-thiocellobiose bound to β-glucosidase from Streptromyces sp. has been studied by 1H-NMR transferred nuclear Overhauser effect spectroscopy (TR-NOE). Thiocellobiose behaves as an inhibitor of this glucosidase when cellobiose is used as substrate. NOE measurements and molecular mechanics calculations have also been performed to estimate the probability distribution of conformers of thiocellobiose when free in solution. Experimental data show that, in contrast with the natural O-analogue, thiocellobiose presents three conformational families in the free state, namely syn, anti-Ψ and anti-Φ whilst only one of them (syn) is recognized by the enzyme.
KW - Molecular mchanics calculation
KW - Streptomyces sp.
KW - Thiocellobiose
KW - Transferred NOE spectroscopy
KW - β-glycosidase
U2 - 10.1016/S0014-5793(97)01571-8
DO - 10.1016/S0014-5793(97)01571-8
M3 - Article
SN - 0014-5793
VL - 421
SP - 243
EP - 248
JO - FEBS Letters
JF - FEBS Letters
ER -