7qbp | pdb_00007qbp

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

spinqualitylabelsall models 7qbp, resolution 1.38Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7qbp is a 1 chain structure with sequence from Saccharopolyspora erythraea NRRL 2338. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.38Å Ligands: FE, MN3, PLM, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RIR2H_SACEN Probable oxidase. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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