7QBP

Crystal structure of R2-like ligand-binding oxidase from Saccharopolyspora Erythraea

Summary for 7QBP

• Entry DOI: 10.2210/pdb7qbp/pdb
• Related: 7QBK
• Descriptor: R2-like ligand binding oxidase, MANGANESE (III) ION, FE (III) ION, ... (6 entities in total)
• Functional Keywords: r2lox, r2-like ligand-binding oxidase, mn/fe cofactor, ribonucleotide reductase r2 subunit fold, metalloprotein, ferritin-like superfamily, oxidoreductase
• Biological source: Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
• Total number of polymer chains: 1
• Total formula weight: 37757.56

Authors

Srinivas, V.,Diamanti, R.,Lebrette, H.,Hogbom, M. (deposition date: 2021-11-19, release date: 2022-04-06, Last modification date: 2024-01-31)

Primary citation

Diamanti, R.,Srinivas, V.,Johansson, A.I.,Nordstrom, A.,Griese, J.J.,Lebrette, H.,Hogbom, M.
Comparative structural analysis provides new insights into the function of R2-like ligand-binding oxidase.
Febs Lett., 596:1600-1610, 2022

PubMed 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 O 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.

PubMed: 35175627
DOI: 10.1002/1873-3468.14319

Experimental method

X-RAY DIFFRACTION (1.38 Å)