9yuw

Crystal structure of sulfoquinovose dioxygenase from Marinobacterium aestuarii in complex with Mn(II), alpha-ketoglutarate, and sulfoquinovose

spinqualitylabelsall models 9yuw, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9yuw is a 1 chain structure with sequence from Marinobacterium aestuarii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: AKG, MN, R7R, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A1A9EZ58_9GAMM Publication Abstract from PubMed Sulfoquinovose dioxygenase (SqoD) enables bacterial carbon assimilation from the abundant sulfosugar sulfoquinovose (SQ) by Fe(ii)/alpha-ketoglutarate (alphaKG)-dependent C-S bond cleavage. Here we report crystal structures of the Marinobacterium aestuarii enzyme (MaSqoD) in multiple states with inert Mn(2+) in place of Fe(2+) (SQ-bound; Mn(2+).alphaKG; Mn(2+).alphaKG.SQ; Mn(2+).succinate), together with steady-state and pre-steady-state kinetics that link the structures with kinetically-inferred intermediates. The X-ray crystal structures show a canonical 2-His-1-carboxylate core metal center with SQ recognition via a mainly neutral network (Gln120, Trp253, backbone carbonyl of Ala185, and backbone amides of Ala89/Met118). Substrate binding triggers a hexacoordinate octahedral-to-pentacoordinate change at the metal center, unveiling a vacant site for O(2) in the fully assembled Mn(2+).alphaKG.SQ complex and thereby curbing uncoupled reactions. Pre-steady-state stopped-flow data support the canonical Fe(iv)[double bond, length as m-dash]O chemistry of the dioxygenase and reveal an additional intermediate consistent with an enzyme-bound alpha-hydroxysulfonate or 6-dehydroglucose species. Together, these findings define the structural and mechanistic basis of sulfolytic SQ catabolism and illuminate the functional repertoire of Fe(ii)/alphaKG-dependent dioxygenases in organosulfur carbon assimilation. Structural and mechanistic basis of sulfolytic C-S bond cleavage by an Fe(ii)/alpha-ketoglutarate-dependent sulfoquinovose dioxygenase.,Lee M, Ho HNN, Maher MJ, Jameson GNL, Williams SJ Chem Sci. 2026 Feb 24;17(16):8100-8107. doi: 10.1039/d5sc09188h. eCollection 2026 , Apr 29. PMID:41777709 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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