Crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C-terminal domain

The thymidylate synthases ThyA and Thy1 are enzymes that catalyse the formation of thymidine monophosphate from 2 ′ -deoxyuridine monophosphate. Thy1 (or ThyX) requires flavin for catalytic reactions, while ThyA does not. In the present study, the crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus HB8 (TtThy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5   Å resolution. TtThy1 is a tetrameric molecule like other Thy1 proteins, to which four FAD molecules are bound. In the crystal of TtThy1, two phosphate ions were bound to each dUMP-binding site. The characteristic feature of TtThy1 is the existence of an extra C-terminal domain (CTD) consisting of three α -helices and a β -strand. The function of the CTD is unknown and database analysis showed that this CTD is only shared by part of the Deinococcus – Thermus phylum.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: flavin-dependent thymidylate synthase pyrimidine nucleotide biosynthetic pathway C-terminal domain research communications Source Type: research