Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 87, Issue 1, Pages 74-80Publisher
WILEY
DOI: 10.1002/prot.25624
Keywords
domain V; glucan-enzyme interactions; GTF-SI; molecular dynamics
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Funding
- Fondo Nacional de Desarrollo Cientifico y Tecnologico [1150704]
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Glucansucrase GTF-SI from Streptococcus mutans is a multidomain enzyme that catalyzes the synthesis of glucan polymers. Domain V locates 100 angstrom from the catalytic site and is required for an optimal activity. Nevertheless, the mechanism governing its functional role remains elusive. In this work, homology modeling and molecular dynamics simulations were employed to examine the effect of domain V in the structure and glucan-binding ability of GTF-SI in full and truncated enzyme models. Our results showed that domain V increases the flexibility of the alpha 4 '-loop-alpha 4 '' motif near the catalytic site resulting in a higher surface for glucan association, and modulates the orientation of a growing oligosaccharide (N=8-23) in glucan-enzyme complexes towards engaging in favorable contacts throughout the protein, whereas in the truncated model the glucan protrudes randomly from domain B towards the solvent. These results are valuable to increase understanding about the functional role of domain V in GH70 glucansucrases.
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