Rajagopal, B.S., Yates, N., Smith, J. et al. (11 more authors) (2024) Structural dissection of two redox proteins from the shipworm symbiont Teredinibacter turnerae. IUCrJ, 11 (Part 2). pp. 260-274. ISSN 2052-2525
Abstract
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | This item is protected by copyright. This is an open-access article distributed under the terms of the Creative Commons Attribution (CC-BY) Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original authors and source are cited. |
Keywords: | shipworms; cellulose; redox proteins; lytic polysaccharide monooxygenases; c-type cytochromes; electron transfers; protein structures; X-ray crystallography; Teredinibacter turnerae |
Dates: |
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Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Funding Information: | Funder Grant number BBSRC (Biotechnology & Biological Sciences Research Council) BB/N019970/1 |
Depositing User: | Symplectic Publications |
Date Deposited: | 12 Feb 2024 11:25 |
Last Modified: | 15 Mar 2024 16:47 |
Status: | Published |
Publisher: | International Union of Crystallography |
Identification Number: | 10.1107/S2052252524001386 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:208995 |