8C4I
Ligand-free Crystal Structure of the decameric Sulfofructose Transaldolase BmSF-TAL
「8BCO」から置き換えられました8C4I の概要
| エントリーDOI | 10.2210/pdb8c4i/pdb |
| 分子名称 | BmSF-TAL (2 entities in total) |
| 機能のキーワード | transaldolase, sulfofugar, decamer, 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 | 253115.57 |
| 構造登録者 | |
| 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 Cited by 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: 36805128DOI: 10.1016/j.str.2023.01.010 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.2 Å) |
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