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Crystal structure of the flavin‐dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C‐terminal domain
Author(s) -
Ogawa Aoba,
Sampei Gen-ichi,
Kawai Gota
Publication year - 2019
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x19007192
Subject(s) - thermus thermophilus , thymidylate synthase , terminal (telecommunication) , chemistry , domain (mathematical analysis) , flavin group , thermus , crystallography , biology , genetics , biochemistry , enzyme , computer science , gene , thermophile , mathematics , fluorouracil , escherichia coli , chemotherapy , telecommunications , mathematical analysis
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.