DOPA formation on tyrosine Y150 of Ribonucleotide reductase QSK R2e variant from Gardnerella vaginalis.

With a crystal structure and mass spectrometry on recombinantly expressed and purified Ribonucleotide reductase QSK R2e variant from Gardnerella vaginalis we show that this protein has a modified DOPA (3,4-Dihydroxy-L-phenylalanine) in the active site analogous to what was observed for the VPK variant. Moreover, we show that this DOPA formation is facilitated by the coexpression of partner proteins NrdI and surprisingly also NrdH and R1 from the same organism.