Abstract
The protein parvulustat (Z-2685) from Streptomyces parvulus comprises 78 amino acids and functions as a highly efficient alpha-amylase inhibitor. Parvulustat shares 29.6 % overall amino acid sequence identity to the well-known alpha-amylase inhibitor tendamistat. Among the conserved residues are the two disulfide bridges (C9-C25, C43-C70) and the active-site motif (W16, R17, Y18). Here, we report the high-resolution NMR structure of parvulustat based on NOEs, J couplings, chemical shifts and hydrogen-exchange data. In addition, we studied the dynamical properties of parvulustat by heteronuclear relaxation measurements. We compare the structure of parvulustat with the structure of tendamistat in terms of secondary structure elements, charges and hydrophobicity. The overall structural composition is very similar, but there are distinct differences including the active-site region. These structural and dynamical differences indicate that for parvulustat an induced-fit mechanism for binding to alpha-amylase might take place, since the structure of tendamistat does not change upon binding to alpha-amylase.
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