9GWW

Crystal structure of sulfoquinovose-1-dehydrogenase from Pseudomonas Putida in complex with sulfoquinovose substrate (sulfo-ED pathway)

9GWW の概要

• エントリーDOI: 10.2210/pdb9gww/pdb
• 分子名称: Sulfoquinovose 1-dehydrogenase, 6-deoxy-6-sulfo-beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: sulfoquinovose; sulfoglycolysis; sulfosugar, short-chain dehydrogenase-reductase; enzyme-substrate complex, oxidoreductase
• 由来する生物種: Pseudomonas putida
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58890.47

構造登録者

Sharma, M.,Davies, G.J. (登録日: 2024-09-27, 公開日: 2025-02-12)

主引用文献

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

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: 39840830
DOI: 10.1042/BCJ20240605

実験手法

X-RAY DIFFRACTION (1.9 Å)