9GWU
Crystal structure of sulfoquinovose-1-dehydrogenase from Pseudomonas Putida (sulfo-ED pathway)
Summary for 9GWU
| Entry DOI | 10.2210/pdb9gwu/pdb |
| Descriptor | Sulfoquinovose 1-dehydrogenase (2 entities in total) |
| Functional Keywords | sulfoquinovose; sulfoglycolysis; short-chain dehydrogenase/reductase; native structure, oxidoreductase |
| Biological source | Pseudomonas putida |
| Total number of polymer chains | 2 |
| Total formula weight | 58646.25 |
| Authors | |
| Primary citation | Burchill, L.,Sharma, M.,Soler, N.M.,Goddard-Borger, E.D.,Davies, G.J.,Williams, S.J. Structure, kinetics, and mechanism of Pseudomonas putida sulfoquinovose dehydrogenase, the first enzyme in the sulfoglycolytic Entner-Doudoroff pathway. Biochem.J., 482:57-72, 2025 Cited by PubMed Abstract: The sulfosugar sulfoquinovose (SQ) is catabolized through the sulfoglycolytic Entner-Doudoroff pathway, beginning with the oxidation of SQ to sulfogluconolactone by SQ dehydrogenase. We present a comprehensive structural and kinetic characterization of Pseudomonas putida SQ dehydrogenase (PpSQDH). PpSQDH is a tetrameric enzyme belonging to the short-chain dehydrogenase/reductase (SDR) superfamily with a strong preference for NAD+ over NADP+. Kinetic analysis revealed a rapid equilibrium ordered mechanism in which the NAD+ cofactor is the first substrate to bind, and NADH is the last product to dissociate. Structural studies revealed a homotetrameric structure in solution and crystals, involving cross-subunit interactions in which the C-terminus residue (Gln260) inserts into the diagonally opposite subunit to form part of the second shell of residues lining the active site. Complexes of PpSQDH with SQ or NAD+ provide insight into the recognition of SQ and together with the kinetic analysis allow the proposal of a catalytic reaction mechanism. Our findings illuminate the mechanism of SQ degradation and the evolution of the SDR superfamily for organosulfonate catabolism. PubMed: 39840830DOI: 10.1042/BCJ20240605 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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