7p07 | pdb_00007p07

Structure of the maltase BaAG2 from Blastobotrys adeninivorans in complex with glucose

spinqualitylabelsall models 7p07, resolution 2.13Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7p07 is a 2 chain structure with sequence from Blastobotrys adeninivorans. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.13Å Ligands: CA, GLC, MB3 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed An early-diverged yeast, Blastobotrys (Arxula) adeninivorans (Ba), has biotechnological potential due to nutritional versatility, temperature tolerance, and production of technologically applicable enzymes. We have biochemically characterized from the Ba type strain (CBS 8244) the GH13-family maltase BaAG2 with efficient transglycosylation activity on maltose. In the current study, transglycosylation of sucrose was studied in detail. The chemical entities of sucrose-derived oligosaccharides were determined using nuclear magnetic resonance. Several potentially prebiotic oligosaccharides with alpha-1,1, alpha-1,3, alpha-1,4, and alpha-1,6 linkages were disclosed among the products. Trisaccharides isomelezitose, erlose, and theanderose, and disaccharides maltulose and trehalulose were dominant transglycosylation products. To date no structure for yeast maltase has been determined. Structures of the BaAG2 with acarbose and glucose in the active center were solved at 2.12 and 2.13 A resolution, respectively. BaAG2 exhibited a catalytic domain with a (beta/alpha)8-barrel fold and Asp216, Glu274, and Asp348 as the catalytic triad. The fairly wide active site cleft contained water channels mediating substrate hydrolysis. Next to the substrate-binding pocket an enlarged space for potential binding of transglycosylation acceptors was identified. The involvement of a Glu (Glu309) at subsite +2 and an Arg (Arg233) at subsite +3 in substrate binding was shown for the first time for alpha-glucosidases. Structural Insight into a Yeast Maltase-The BaAG2 from Blastobotrys adeninivorans with Transglycosylating Activity.,Ernits K, Kjeldsen C, Persson K, Grigor E, Alamae T, Visnapuu T J Fungi (Basel). 2021 Sep 29;7(10). pii: jof7100816. doi: 10.3390/jof7100816. PMID:34682239 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Alpha-glucosidase 3D structures

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