The glycoside hydrolase family 39 (GH39) is a functionally expanding family with limited understanding about the molecular basis for substrate specificity and extremophilicity. In this work, we demonstrate the key role of the positive-subsite region in modulating substrate affinity and how the lack of a C-terminal extension impacts on oligomerization and structural stability of some GH39 members. The crystallographic and SAXS structures of a new GH39 member from the phytopathogen support the importance of an extended C-terminal to promote oligomerization as a molecular strategy to enhance thermal stability.
View Article and Find Full Text PDFThe chemical properties of materials are dependent on dynamic changes in their three-dimensional (3D) structure as well as on the reactive environment. We report an 3D imaging study of defect dynamics of a single gold nanocrystal. Our findings offer an insight into its dynamic nanostructure and unravel the formation of a nanotwin network under CO oxidation conditions.
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