9W7A
Crystal structure of L-galactose dehydrogenase from Luteolibacter sp. strain LG18 in complex with L-glucose and NADP+
Summary for 9W7A
| Entry DOI | 10.2210/pdb9w7a/pdb |
| Descriptor | L-galactose dehydrogenase, beta-L-glucopyranose, NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
| Functional Keywords | dehydrogenase, oxidoreductase |
| Biological source | Luteolibacter sp. LG18 |
| Total number of polymer chains | 2 |
| Total formula weight | 77753.14 |
| Authors | Koubara, K.,Takenoya, M.,Suzuki, M.,Ito, S.,Sasaki, Y.,Nakamura, A.,Yajima, S. (deposition date: 2025-08-06, release date: 2026-04-01) |
| Primary citation | Koubara, K.,Kim, M.,Takenoya, M.,Nakanishi, A.,Suzuki, M.,Azuma, S.,Ito, S.,Sasaki, Y.,Nakamura, A.,Yajima, S. Characterization of bacterial l-galactose dehydrogenase with l-glucose dehydrogenase activity from Luteolibacter sp. strain LG18. Biosci.Biotechnol.Biochem., 2026 Cited by PubMed Abstract: The crystal structure of l-galactose dehydrogenase (LGDH) with l-glucose dehydrogenase activity from Luteolibacter sp. strain LG18 (Lu-LGDH) was determined in complex with l-galactose or l-glucose and NADP⁺. This structural analysis identified key residues involved in substrate binding, and alanine-substituted mutants demonstrated the roles of these residues, including Tyr56, acting as potential general base within the catalytic tetrad. Unlike plant enzymes that show a preference for NAD⁺, Lu-LGDH exhibits a marked preference for NADP⁺ as a cofactor. This preference was attributed to the interaction of the phosphate group with Arg28, Thr269, and Asn274. The binding mode of l-glucose was similar to that of l-galactose. The C4 hydroxyl group (the structural difference between these pyranoses) was not used for substrate binding, which explains the dual activity of the enzyme. Furthermore, among the substrate-binding residues that were mutated, Arg308, which is not conserved among LGDHs, was crucial for the enzymatic activity. PubMed: 41854348DOI: 10.1093/bbb/zbag041 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.56 Å) |
Structure validation
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