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Cellvibrio japonicus α-L-arabinanase 43A has a novel five-blade β-propeller fold

Abstract

Cellvibrio japonicus arabinanase Arb43A hydrolyzes the α-1,5-linked L-arabinofuranoside backbone of plant cell wall arabinans. The three-dimensional structure of Arb43A, determined at 1.9 Å resolution, reveals a five-bladed β-propeller fold. Arb43A is the first enzyme known to display this topology. A long V-shaped surface groove, partially enclosed at one end, forms a single extended substrate-binding surface across the face of the propeller. Three carboxylates deep in the active site groove provide the general acid and base components for glycosidic bond hydrolysis with inversion of anomeric configuration.

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Figure 1: Comparison of the three-dimensional structure of Arb43A and tachylectin.
Figure 2: The reaction catalyzed by Arb43A.
Figure 3: Three-dimensional structure of Arb43A in complex with substrate.

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Acknowledgements

We thank the BBSRC and the Wellcome Trust for funding and the staff of the Daresbury and European Synchrotron Radiation Sources for provision of beamtime. D.N. thanks EMBO for provision of a long-term fellowship and G.J.D is a Royal Society University Research Fellow.

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Correspondence to Gideon J. Davies.

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Nurizzo, D., Turkenburg, J., Charnock, S. et al. Cellvibrio japonicus α-L-arabinanase 43A has a novel five-blade β-propeller fold. Nat Struct Mol Biol 9, 665–668 (2002). https://doi.org/10.1038/nsb835

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