Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase.

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Diamanti R, Srinivas V, Johansson AI, Nordström A, Griese JJ, Lebrette H, Högbom M

FEBS Lett. 596 (12) 1600-1610 [2022-06-00; online 2022-03-04]

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.

Swedish Metabolomics Centre (SMC) [Collaborative]

PubMed 35175627

DOI 10.1002/1873-3468.14319

Crossref 10.1002/1873-3468.14319

pmc: PMC9314684
RefSeq: WP_011277966
RefSeq: WP_009945174
RefSeq: yp_148624
RefSeq: WP_011278976