Crystal structure of the flavin‐dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C‐terminal domain. Issue 6 (17th June 2019)

• Record Type: Journal Article
• Authors: Ogawa, Aoba; Sampei, Gen-ichi; Kawai, Gota
• Is Part Of: Acta crystallographica. Volume 75:Issue 6(2019:Jun.)
• Page Start: 450
• Page End: 454
• Publication Date: 2019-06-17
• Subjects: flavin‐dependent thymidylate synthase -- pyrimidine nucleotide biosynthetic pathway -- C‐terminal domain; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X19007192
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The crystal structure of the flavin‐dependent thymidylate synthase Thy1 from Thermus thermophilus HB8 ( Tt Thy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5 Å resolution. Tt Thy1 is a tetrameric molecule, to which four FAD molecules are bound. Two phosphate ions were bound to each dUMP‐binding site. The characteristic feature of Tt Thy1 is the existence of an extra C‐terminal domain (CTD) consisting of three α‐helices and a β‐strand. 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 ( Tt Thy1, TTHA1096) was determined in complex with FAD and phosphate at 2.5 Å resolution. Tt Thy1 is a tetrameric molecule like other Thy1 proteins, to which four FAD molecules are bound. In the crystal of Tt Thy1, two phosphate ions were bound to each dUMP‐binding site. The characteristic feature of Tt Thy1 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.