Structural analysis of Borrelia  burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection

The periplasmic lipoprotein BB0365 of the Lyme disease agentBorrelia burgdorferi is expressed throughout mammalian infection and is essential for all phases of Lyme disease infection; its function, however, remains unknown. In the current study, our structural analysis of BB0365 revealed the same structural fold as that found in the NqrC and RnfG subunits of the NADH:quinone and ferredoxin:NAD+ sodium ‐translocating oxidoreductase complexes, which points to a potential role for BB0365 as a component of the sodium pump. Additionally, BB0365 coordinated Zn2+ by the His51, His55, His140 residues, and the Zn2+‐binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein forB.  burgdorferi to cause Lyme disease.

Source: FEBS Letters - September 12, 2019 Category: Biochemistry Authors: Kalvis Brangulis, Inara Akopjana, Ivars Petrovskis, Andris Kazaks, Atis Jekabsons, Kristaps Jaudzems, Arturs Viksna, Maris Bertins, Kaspars Tars Tags: Research Article Source Type: research