Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase. Diamanti, R., Srinivas, V., Johansson, A. I., Nordström, A., Griese, J. J., Lebrette, H., & Högbom, M. FEBS Letters, 596(12):1600–1610, 2022. _eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14319![Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase [link]](https://bibbase.org/img/filetypes/link.svg "link")
Paper doi abstract bibtex 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.
@article{diamanti_comparative_2022,
title = {Comparative structural analysis provides new insights into the function of {R2}-like ligand-binding oxidase},
volume = {596},
copyright = {© 2022 The Authors. FEBS Letters published by John Wiley \& Sons Ltd on behalf of Federation of European Biochemical Societies},
issn = {1873-3468},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/1873-3468.14319},
doi = {10.1002/1873-3468.14319},
abstract = {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.},
language = {en},
number = {12},
urldate = {2022-06-30},
journal = {FEBS Letters},
author = {Diamanti, Riccardo and Srinivas, Vivek and Johansson, Annika I. and Nordström, Anders and Griese, Julia J. and Lebrette, Hugo and Högbom, Martin},
year = {2022},
note = {\_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/1873-3468.14319},
keywords = {R2-like ligand-binding oxidase, R2lox, aldehyde deformylating oxygenase, ferritin-like protein, hydroxy fatty acids, long-chain fatty acids},
pages = {1600--1610},
}
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