Domain flexibility of a glucansucrase and shape of the full-length enzyme
What is it about?
The structure of N-terminally truncated glucansucrase GTF180-ΔN from Lactobacillus reuteri 180 in a second crystal form reveals that domains V can adopt completely different positions. SAXS experiments with GTF180-ΔN and the full-length GTF180 confirm this positional variability, and show that conformational flexibility, which may be a general feature of glucansucrases, occurs in solution.
Why is it important?
The article shows for the first time the shape of a full-length glucansucrase (~1600 amino acids) and the flexibility of its domains.
The following have contributed to this page: Professor Lubbert Dijkhuizen and Bauke Dijkstra
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