Flexibility of truncated and full-length glucansucrase GTF180 enzymes fromLactobacillus reuteri180

Tjaard Pijning, Andreja Vujičić-Žagar, Slavko Kralj, Lubbert Dijkhuizen, Bauke W. Dijkstra
  • FEBS Journal, March 2014, Wiley
  • DOI: 10.1111/febs.12769

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.

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The following have contributed to this page: Professor Lubbert Dijkhuizen and Bauke Dijkstra