8JSV
Dihydrofolate reductase-like enzyme from Leptospira interrogans (selenomethionine derivative)
Summary for 8JSV
| Entry DOI | 10.2210/pdb8jsv/pdb |
| Descriptor | Dihydrofolate reductase family protein, PENTAETHYLENE GLYCOL, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (5 entities in total) |
| Functional Keywords | dihydrofolate reductase-like enzyme, oxidoreductase, spirochete |
| Biological source | Leptospira interrogans serovar Pomona |
| Total number of polymer chains | 10 |
| Total formula weight | 243837.95 |
| Authors | Chandit, C.,Wangkanont, K. (deposition date: 2023-06-20, release date: 2024-06-26, Last modification date: 2025-02-05) |
| Primary citation | 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 Cited by 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: 39824401DOI: 10.1016/j.ijbiomac.2025.139931 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.55 Å) |
Structure validation
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