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Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae

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.

Publication metadata

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


DOI: 10.1107/S2052252524001386


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