3GBD
Crystal structure of the isomaltulose synthase SmuA from Protaminobacter rubrum
Summary for 3GBD
| Entry DOI | 10.2210/pdb3gbd/pdb |
| Related | 3GBE |
| Descriptor | Sucrose isomerase SmuA from Protaminobacter rubrum, 1,2-ETHANEDIOL, CITRATE ANION, ... (4 entities in total) |
| Functional Keywords | sucrose isomerase, glycoside hydrolase, protaminobacter rubrum, isomerase |
| Biological source | Protaminobacter rubrum |
| Total number of polymer chains | 1 |
| Total formula weight | 66374.00 |
| Authors | Ravaud, S.,Robert, X.,Haser, R.,Aghajari, N. (deposition date: 2009-02-19, release date: 2009-05-26, Last modification date: 2023-11-01) |
| Primary citation | Ravaud, S.,Robert, X.,Watzlawick, H.,Haser, R.,Mattes, R.,Aghajari, N. Structural determinants of product specificity of sucrose isomerases Febs Lett., 583:1964-1968, 2009 Cited by PubMed Abstract: The healthy sweetener isomaltulose is industrially produced from the conversion of sucrose by the sucrose isomerase SmuA from Protaminobacter rubrum. Crystal structures of SmuA in native and deoxynojirimycin complexed forms completed with modeling studies unravel the characteristics of the isomaltulose synthases catalytic pocket and their substrate binding mode. Comparison with the trehalulose synthase MutB highlights the role of Arg(298) and Arg(306) active site residues and surface charges in controlling product specificity of sucrose isomerases (isomaltulose versus trehalulose). The results provide a rationale for the specific design of optimized enzymes. PubMed: 19427862DOI: 10.1016/j.febslet.2009.05.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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