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- PDB-8c4i: Ligand-free Crystal Structure of the decameric Sulfofructose Tran... -
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Basic information
Entry | Database: PDB / ID: 8c4i | |||||||||
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Title | Ligand-free Crystal Structure of the decameric Sulfofructose Transaldolase BmSF-TAL | |||||||||
![]() | BmSF-TAL | |||||||||
![]() | TRANSFERASE / Transaldolase / Sulfofugar / Decamer | |||||||||
Function / homology | 6-deoxy-6-sulfo-D-fructose transaldolase / Transaldolase/Fructose-6-phosphate aldolase, archaeal/bacterial / transaldolase activity / Transaldolase/Fructose-6-phosphate aldolase / Transaldolase/Fructose-6-phosphate aldolase / aldehyde-lyase activity / Aldolase-type TIM barrel / carbohydrate metabolic process / 6-deoxy-6-sulfo-D-fructose transaldolase![]() | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Snow, A.J.D. / Sharma, M. / Davies, G.J. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and mechanism of sulfofructose transaldolase, a key enzyme in sulfoquinovose metabolism. Authors: Alexander J D Snow / Mahima Sharma / Palika Abayakoon / Spencer J Williams / James N Blaza / Gideon J Davies / ![]() ![]() 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 ...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. | |||||||||
History |
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-Validation report
Summary document | ![]() | 495 KB | Display | ![]() |
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Full document | ![]() | 529.2 KB | Display | |
Data in XML | ![]() | 75.6 KB | Display | |
Data in CIF | ![]() | 101 KB | Display | |
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-Related structure data
Related structure data | ![]() 8bc2C ![]() 8bc3C ![]() 8bc4C C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Assembly
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Noncrystallographic symmetry (NCS) | NCS domain:
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