Functional characterization of heat-shock protein 90 from Oryza sativa and crystal structure of its N-terminal domain

In this study, biochemical characterization of an Hsp90 protein from rice (Oryza sativa; OsHsp90) has been performed and the crystal structure of its N-terminal domain (OsHsp90-NTD) was determined. The binding of OsHsp90 to its substrate ATP and the inhibitor 17-AAG was studied by fluorescence spectroscopy. The protein also exhibited a weak ATPase activity. The crystal structure of OsHsp90-NTD was solved in complex with the nonhydrolyzable ATP analogue AMPPCP at 3.1 Å resolution. The domain was crystallized by cross-seeding with crystals of the N-terminal domain of Hsp90 from Dictyostelium discoideum, which shares 70% sequence identity with OsHsp90-NTD. This is the second reported structure of a domain of Hsp90 from a plant source.

Source: Acta Crystallographica Section F - May 20, 2015 Category: Biochemistry Authors: Raman, S.Suguna, K. Tags: Hsp90 Oryza sativa 17-AAG ATPase activity cross-seeding research communications Source Type: research