8cip

Crystal structure of transketolase from Geobacillus stearothermophilus

spinqualitylabelsall models 8cip, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8cip is a 4 chain structure with sequence from Geobacillus stearothermophilus. 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: ACT, CL, EDO, MG, TPP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function TKT_GEOSE Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, likely via a covalent intermediate with the cofactor thiamine pyrophosphate. Can use L-erythrulose as donor and D-ribose-5-phosphate as acceptor substrates, forming glycolaldehyde and D-sedoheptulose-7-phosphate. For synthetic purposes, is able to use hydroxypyruvate (HPA) as donor substrate, making the reaction irreversible due to the release of carbon dioxide, and various aldehydes as acceptor substrates, which leads to the corresponding ketoses. Thus, using hydroxypyruvate as donor and three different aldehydes as acceptors, i.e. glycolaldehyde, D-glyceraldehyde and butyraldehyde, the enzyme stereoselectively forms the corresponding products L-erythrulose, D-xylulose and (3S)-1,3-dihydroxyhexan-2-one, respectively.[REFERENCE:2] See Also Transketolase 3D structures

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