6S9V
Crystal structure of sucrose 6F-phosphate phosphorylase from Thermoanaerobacter thermosaccharolyticum
Summary for 6S9V
| Entry DOI | 10.2210/pdb6s9v/pdb |
| Descriptor | Sucrose 6(F)-phosphate phosphorylase, 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | glycoside phosphorylase, sucrose 6-phosphate, glycoside hydrolase family gh13-18, transferase |
| Biological source | Thermoanaerobacterium thermosaccharolyticum DSM 571 |
| Total number of polymer chains | 2 |
| Total formula weight | 118730.75 |
| Authors | Capra, N.,Franceus, J.,Desmet, T.,Thunnissen, A.M.W.H. (deposition date: 2019-07-15, release date: 2019-08-28, Last modification date: 2024-01-24) |
| Primary citation | Franceus, J.,Capra, N.,Desmet, T.,Thunnissen, A.W.H. Structural Comparison of a Promiscuous and a Highly Specific Sucrose 6 F -Phosphate Phosphorylase. Int J Mol Sci, 20:-, 2019 Cited by PubMed Abstract: In family GH13 of the carbohydrate-active enzyme database, subfamily 18 contains glycoside phosphorylases that act on α-sugars and glucosides. Because their phosphorolysis reactions are effectively reversible, these enzymes are of interest for the biocatalytic synthesis of various glycosidic compounds. Sucrose 6-phosphate phosphorylases (SPPs) constitute one of the known substrate specificities. Here, we report the characterization of an SPP from with a far stricter specificity than the previously described promiscuous SPP from . Crystal structures of both SPPs were determined to provide insight into their similarities and differences. The residues responsible for binding the fructose 6-phosphate group in subsite +1 were found to differ considerably between the two enzymes. Furthermore, several variants that introduce a higher degree of substrate promiscuity in the strict SPP from were designed. These results contribute to an expanded structural knowledge of enzymes in subfamily GH13_18 and facilitate their rational engineering. PubMed: 31405215DOI: 10.3390/ijms20163906 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.83 Å) |
Structure validation
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