8JT0

Dihydrofolate reductase-like enzyme from Leptospira interrogans with additional NADP+

8JT0 の概要

• エントリーDOI: 10.2210/pdb8jt0/pdb
• 分子名称: Dihydrofolate reductase family protein, PENTAETHYLENE GLYCOL, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (6 entities in total)
• 機能のキーワード: dihydrofolate reductase-like enzyme, oxidoreductase, spirochete
• 由来する生物種: Leptospira interrogans serovar Pomona
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 240528.83

構造登録者

Wangkanont, K. (登録日: 2023-06-20, 公開日: 2024-06-26, 最終更新日: 2025-02-05)

主引用文献

Chandit, C.,Hengphasatporn, K.,Donsuy, P.,Shigeta, Y.,Wangkanont, K.
Structure and catalytic activity of a dihydrofolate reductase-like enzyme from Leptospira interrogans.
Int.J.Biol.Macromol., 298:139931-139931, 2025

PubMed Abstract: A dihydrofolate reductase (DHFR)-like enzyme from Leptospira interrogans (LiDHFRL) was cloned and the recombinant protein was characterized. Sequence alignment suggested that the enzyme lacked the conserved catalytic residues found in DHFR. Indeed, LiDHFRL did not catalyze the reduction of dihydrofolate by either NADH or NADPH. X-ray crystallography revealed that LiDHFRL bound NADP(H) tightly, but its active site architecture was vastly different from that of Escherichia coli DHFR (EcDHFR) and other DHFRLs. Interestingly, vanillin could serve as a substrate for LiDHFRL, demonstrating that LiDHFRL is a functional enzyme. A putative vanillin binding mode was proposed.

PubMed: 39824401
DOI: 10.1016/j.ijbiomac.2025.139931

実験手法

X-RAY DIFFRACTION (2.2 Å)