5N7J
Crystal structure of Neisseria polysaccharea amylosucrase mutant efficient for the synthesis of controlled size maltooligosaccharides
Summary for 5N7J
| Entry DOI | 10.2210/pdb5n7j/pdb |
| Related PRD ID | PRD_900003 PRD_900009 |
| Descriptor | Amylosucrase, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | amylosucrase, glycoside hydrolase, glucosyl transferase, mutant, neisseria polysaccharea, gh13, hydrolase |
| Biological source | Neisseria polysaccharea |
| Cellular location | Secreted : Q9ZEU2 |
| Total number of polymer chains | 1 |
| Total formula weight | 73818.25 |
| Authors | Verges, A.,Tranier, S. (deposition date: 2017-02-20, release date: 2017-06-28, Last modification date: 2024-01-17) |
| Primary citation | Verges, A.,Barbe, S.,Cambon, E.,Moulis, C.,Tranier, S.,Remaud-Simeon, M.,Andre, I. Engineering of anp efficient mutant of Neisseria polysaccharea amylosucrase for the synthesis of controlled size maltooligosaccharides. Carbohydr Polym, 173:403-411, 2017 Cited by PubMed Abstract: Amylosucrase from Neisseria polysaccharea naturally catalyzes the synthesis of α-1,4 glucans from sucrose. The product profile is quite polydisperse, ranging from soluble chains called maltooligosaccharides to high-molecular weight insoluble amylose. This enzyme was recently subjected to engineering of its active site to enable recognition of non-natural acceptor substrates. Libraries of variants were constructed and screened on sucrose, allowing the identification of a mutant that showed a 6-fold enhanced activity toward sucrose compared to the wild-type enzyme. Furthermore, its product profile was unprecedented, as only soluble maltooligosaccharides of controlled size chains (2 DOI: 10.1016/j.carbpol.2017.06.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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