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Lookup NU author(s): Dr Catherine Tétard-Jones, Professor William WillatsORCiD
This work is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
© 2024 International Union of Crystallography. All rights reserved.The discovery of lytic polysaccharide monooxygenases (LPMOs), a family of copper-dependent enzymes that play a major role in polysaccharide degradation, has revealed the importance of oxidoreductases in the biological utilization of biomass. In fungi, a range of redox proteins have been implicated as working in harness with LPMOs to bring about polysaccharide oxidation. In bacteria, less is known about the interplay between redox proteins and LPMOs, or how the interaction between the two contributes to polysaccharide degradation. We therefore set out to characterize two previously unstudied proteins from the shipworm symbiont Teredinibacter turnerae that were initially identified by the presence of carbohydrate binding domains appended to uncharacterized domains with probable redox functions. Here, X-ray crystal structures of several domains from these proteins are presented together with initial efforts to characterize their functions. The analysis suggests that the target proteins are unlikely to function as LPMO electron donors, raising new questions as to the potential redox functions that these large extracellular multi-haem-containing c-type cytochromes may perform in these bacteria.
Author(s): Rajagopal BS, Yates N, Smith J, Paradisi A, Tetard-Jones C, Willats WGT, Marcus S, Knox JP, Firdaus-Raih M, Henrissat B, Davies GJ, Walton PH, Parkin A, Hemsworth GR
Publication type: Article
Publication status: Published
Journal: IUCrJ
Year: 2024
Volume: 11
Issue: 2
Pages: 260-274
Online publication date: 01/03/2024
Acceptance date: 12/02/2024
Date deposited: 25/03/2024
ISSN (electronic): 2052-2525
Publisher: International Union of Crystallography
URL: https://doi.org/10.1107/S2052252524001386
DOI: 10.1107/S2052252524001386
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