Functional and Structural Characterization of α-(1→2) Branching Sucrase Derived from DSR-E Glucansucrase

Yoann Brison (1) , Tjaard Pijning (2) , Yannick Malbert (1) , Émeline Fabre (1) , Lionel Mourey (3) , Sandrine Morel (1) , Gabrielle Potocki-Veronese (1) , Pierre Monsan (1) , Samuel Tranier (3) , Magali Remaud-Siméon (1) , Bauke W Dijkstra (2)

1 LISBP - Laboratoire d'Ingénierie des Systèmes Biologiques et des Procédés
2 University of Groningen [Groningen]
3 IPBS - Institut de pharmacologie et de biologie structurale

Background: The transglucosidase GBD-CD2 shows a unique ␣-(132) branching specificity among GH70 family members when catalyzing dextran glucosylation from sucrose. Results: The truncated form ⌬N 123-GBD-CD2 was biochemically studied and structurally characterized at 1.90 Å resolution. Conclusion: Dextran recognition and regiospecificity clearly involves a residue in subsite ϩ1. Significance: This is the first three-dimensional structure of a GH70 enzyme that reveals determinants of ␣-(132) linkage specificity.

Domaines: Sciences du Vivant [q-bio]

Yoann Brison, Tjaard Pijning, Yannick Malbert, Émeline Fabre, Lionel Mourey, et al.. Functional and Structural Characterization of α-(1→2) Branching Sucrase Derived from DSR-E Glucansucrase. Journal of Biological Chemistry, 2012, 287, pp.7915 - 7924. ⟨10.1074/jbc.m111.305078⟩. ⟨hal-03003060⟩