6J61

Crystal Structure of Thymidylate Synthase, Thy1, from Thermus thermophilus having an Extra C Terminal Domain

Summary for 6J61

• Entry DOI: 10.2210/pdb6j61/pdb
• Descriptor: Flavin-dependent thymidylate synthase, FLAVIN-ADENINE DINUCLEOTIDE, PHOSPHATE ION, ... (4 entities in total)
• Functional Keywords: thymidylate synthase, pyrimidine nucleotide biosynthetic pathway, c-terminal domain, structural genomics, transferase
• Biological source: Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
• Total number of polymer chains: 4
• Total formula weight: 128113.44

Authors

Ogawa, A.,Sampei, G.,Kawai, G. (deposition date: 2019-01-12, release date: 2019-06-26, Last modification date: 2023-11-22)

Primary citation

Ogawa, A.,Sampei, G.,Kawai, G.
Crystal structure of the flavin-dependent thymidylate synthase Thy1 from Thermus thermophilus with an extra C-terminal domain.
Acta Crystallogr.,Sect.F, 75:450-454, 2019

PubMed 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.

PubMed: 31204692
DOI: 10.1107/S2053230X19007192

Experimental method

X-RAY DIFFRACTION (2.5 Å)