8BC2

Ligand-Free Structure of the decameric sulfofructose transaldolase BmSF-TAL

8BC2 の概要

• エントリーDOI: 10.2210/pdb8bc2/pdb
• EMDBエントリー: 15960
• 分子名称: Transaldolase (2 entities in total)
• 機能のキーワード: transaldolase, cryo-em, decamer, sulfofructose, transferase
• 由来する生物種: Bacillus aryabhattai
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 244435.45

構造登録者

Snow, A.J.D.,Sharma, M.,Blaza, J.,Davies, G.J. (登録日: 2022-10-14, 公開日: 2023-01-18, 最終更新日: 2025-07-09)

主引用文献

Snow, A.J.D.,Sharma, M.,Abayakoon, P.,Williams, S.J.,Blaza, J.N.,Davies, G.J.
Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism.
Structure, 31:244-, 2023

PubMed Abstract: 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.

PubMed: 36805128
DOI: 10.1016/j.str.2023.01.010

実験手法

ELECTRON MICROSCOPY (2.6 Å)