6F6E

R2-like ligand-binding oxidase V72A mutant with anaerobically reconstituted Mn/Fe cofactor

Summary for 6F6E

• Entry DOI: 10.2210/pdb6f6e/pdb
• Related: 4HR0 4HR4 4HR5 4XB9 4XBV 4XBW 5DCO 5DCR 5DCS 5EKB 5OMJ 5OMK 6F65 6F6B 6F6C 6F6F 6F6G 6F6H 6F6K 6F6L 6F6M
• Descriptor: Ribonucleotide reductase small subunit, FE (II) ION, MANGANESE (II) ION, ... (5 entities in total)
• Functional Keywords: r2-like ligand-binding oxidase, mn/fe cofactor, ribonucleotide reductase r2 subunit fold, metalloprotein oxidoreductase, oxidoreductase
• Biological source: Geobacillus kaustophilus (strain HTA426)
• Total number of polymer chains: 2
• Total formula weight: 74715.61

Authors

Griese, J.J.,Hogbom, M. (deposition date: 2017-12-05, release date: 2018-07-04, Last modification date: 2024-01-17)

Primary citation

Griese, J.J.,Branca, R.M.M.,Srinivas, V.,Hogbom, M.
Ether cross-link formation in the R2-like ligand-binding oxidase.
J. Biol. Inorg. Chem., 23:879-886, 2018

PubMed Abstract: R2-like ligand-binding oxidases contain a dinuclear metal cofactor which can consist either of two iron ions or one manganese and one iron ion, but the heterodinuclear Mn/Fe cofactor is the preferred assembly in the presence of Mn and Fe in vitro. We have previously shown that both types of cofactor are capable of catalyzing formation of a tyrosine-valine ether cross-link in the protein scaffold. Here we demonstrate that Mn/Fe centers catalyze cross-link formation more efficiently than Fe/Fe centers, indicating that the heterodinuclear cofactor is the biologically relevant one. We further explore the chemical potential of the Mn/Fe cofactor by introducing mutations at the cross-linking valine residue. We find that cross-link formation is possible also to the tertiary beta-carbon in an isoleucine, but not to the secondary beta-carbon or tertiary gamma-carbon in a leucine, nor to the primary beta-carbon of an alanine. These results illustrate that the reactivity of the cofactor is highly specific and directed.

PubMed: 29946980
DOI: 10.1007/s00775-018-1583-3

Experimental method

X-RAY DIFFRACTION (1.627 Å)