AI Article Synopsis
- ThyA and Thy1 are thymidylate synthase enzymes that convert deoxyuridine monophosphate to thymidine monophosphate, with Thy1 requiring flavin for its function.
- The crystal structure of Thy1 from Thermus thermophilus was determined, revealing it as a tetramer with four FAD molecules and two bound phosphate ions at the dUMP-binding sites.
- An additional unique C-terminal domain (CTD) was identified in TtThy1, consisting of three α-helices and a β-strand, though its function remains unknown and is specific to certain species within the Deinococcus-Thermus phylum.
Article Abstract
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.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572101 | PMC |
| http://dx.doi.org/10.1107/S2053230X19007192 | DOI Listing |
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