Structural highlights
Function
Q4J9R6_SULAC
Publication Abstract from PubMed
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 A and 2.26 A resolution, respectively, providing the highest resolution structure for R2lox, as well as new insights into putative mechanisms regulating the function of the enzyme.
Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase.,Diamanti R, Srinivas V, Johansson AI, Nordstrom A, Griese JJ, Lebrette H, Hogbom M FEBS Lett. 2022 Feb 17. doi: 10.1002/1873-3468.14319. PMID:35175627[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Diamanti R, Srinivas V, Johansson AI, Nordstrom A, Griese JJ, Lebrette H, Hogbom M. Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase. FEBS Lett. 2022 Feb 17. doi: 10.1002/1873-3468.14319. PMID:35175627 doi:http://dx.doi.org/10.1002/1873-3468.14319
