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Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

Biology

Structure and dynamics of an α-fucosidase reveal a mechanism for highly efficient IgG transfucosylation

E. H. Klontz, C. Li, et al.

Discover the fascinating world of fucosylation with the groundbreaking research from Erik H. Klontz and colleagues. Their study delves into the unique properties of AlfC, an α-fucosidase from *Lactobacillus casei*, revealing its mechanism through crystal structures and molecular dynamics. Uncover how this enzyme's specificity can impact protein functions and the potential for creating transfucosidase mutants.

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Playback language: English
Abstract
Fucosylation is crucial for various protein functions. AlfC, an α-fucosidase from *Lactobacillus casei*, displays high specificity for α(1,6)-fucose linkages. This study uses crystal structures, mutational and kinetic analyses, and molecular dynamics to elucidate AlfC's mechanism. Results suggest an aromatic subsite for GlcNAc accommodation, activity control via active-site loop conformations, and a framework for creating AlfC transfucosidase mutants.
Publisher
NATURE COMMUNICATIONS
Published On
Dec 04, 2020
Authors
Erik H. Klontz, Chao Li, Kyle Kihn, James K. Fields, Dorothy Beckett, Greg A. Snyder, Patrick L. Wintrode, Daniel Deredge, Lai-Xi Wang, Eric J. Sundberg
Tags
fucosylation
α-fucosidase
Lactobacillus casei
crystal structures
molecular dynamics

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