Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism.

Autor:	Snow AJD; Department of Chemistry, York Structural Biology Laboratory, York YO10 5DD, UK., Sharma M; Department of Chemistry, York Structural Biology Laboratory, York YO10 5DD, UK., Abayakoon P; School of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia., Williams SJ; School of Chemistry, University of Melbourne, Parkville, VIC 3010, Australia; Bio21 Molecular Science and Biotechnology Institute, University of Melbourne, Parkville, VIC 3010, Australia. Electronic address: sjwill@unimelb.edu.au., Blaza JN; Department of Chemistry, York Structural Biology Laboratory, York YO10 5DD, UK. Electronic address: jamie.blaza@york.ac.uk., Davies GJ; Department of Chemistry, York Structural Biology Laboratory, York YO10 5DD, UK. Electronic address: gideon.davies@york.ac.uk.
Jazyk:	angličtina
Zdroj:	Structure (London, England : 1993) [Structure] 2023 Mar 02; Vol. 31 (3), pp. 244-252.e4. Date of Electronic Publication: 2023 Feb 17.
DOI:	10.1016/j.str.2023.01.010
Abstrakt:	Sulfoquinovose (SQ) is a key component of plant sulfolipids (sulfoquinovosyl diacylglycerols) and a major environmental reservoir of biological sulfur. Breakdown of SQ is achieved by bacteria through the pathways of sulfoglycolysis. The sulfoglycolytic sulfofructose transaldolase (sulfo-SFT) pathway is used by gut-resident firmicutes and soil saprophytes. After isomerization of SQ to sulfofructose (SF), the namesake enzyme catalyzes the transaldol reaction of SF transferring dihydroxyacetone to 3C/4C acceptors to give sulfolactaldehyde and fructose-6-phosphate or sedoheptulose-7-phosphate. We report the 3D cryo-EM structure of SF transaldolase from Bacillus megaterium in apo and ligand bound forms, revealing a decameric structure formed from two pentameric rings of the protomer. We demonstrate a covalent "Schiff base" intermediate formed by reaction of SF with Lys89 within a conserved Asp-Lys-Glu catalytic triad and defined by an Arg-Trp-Arg sulfonate recognition triad. The structural characterization of the signature enzyme of the sulfo-SFT pathway provides key insights into molecular recognition of the sulfonate group of sulfosugars. Competing Interests: Declaration of interests The authors declare no competing interests. (Copyright © 2023 The Author(s). Published by Elsevier Ltd.. All rights reserved.)
Databáze:	MEDLINE
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