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Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
Umeå University, Faculty of Science and Technology, Department of Plant Physiology. Swedish Metabolomics Centre.ORCID iD: 0000-0001-5000-1288
Umeå University, Faculty of Science and Technology, Department of Plant Physiology.ORCID iD: 0000-0003-3676-817X
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2022 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 596, no 12, p. 1600-1610Article in journal (Refereed) Published
Abstract [en]

R2-like ligand-binding oxidase (R2lox) is a ferritin-like protein that harbours a heterodinuclear manganese–iron active site. Although R2lox function is yet to be established, the enzyme binds a fatty acid ligand coordinating the metal centre and catalyses the formation of a tyrosine–valine ether cross-link in the protein scaffold upon O2 activation. Here, we characterized the ligands copurified with R2lox by mass spectrometry-based metabolomics. Moreover, we present the crystal structures of two new homologs of R2lox, from Saccharopolyspora erythraea and Sulfolobus acidocaldarius, at 1.38 Å and 2.26 Å resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.

Place, publisher, year, edition, pages
John Wiley & Sons, 2022. Vol. 596, no 12, p. 1600-1610
Keywords [en]
aldehyde deformylating oxygenase, ferritin-like protein, hydroxy fatty acids, long-chain fatty acids, R2-like ligand-binding oxidase, R2lox
National Category
Biochemistry and Molecular Biology Structural Biology
Identifiers
URN: urn:nbn:se:umu:diva-193164DOI: 10.1002/1873-3468.14319ISI: 000764082200001PubMedID: 35175627Scopus ID: 2-s2.0-85126047671OAI: oai:DiVA.org:umu-193164DiVA, id: diva2:1645657
Funder
Knut and Alice Wallenberg Foundation, 2017.0275Knut and Alice Wallenberg Foundation, 2019.0436Swedish Research Council, 2017-0401EU, European Research Council, 724394Available from: 2022-03-18 Created: 2022-03-18 Last updated: 2022-11-24Bibliographically approved

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Johansson, Annika I.Nordström, Anders

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