6R1G

Crystal structure of Borrelia burgdorferi periplasmic protein BB0365 (IPLA7, p22)

Summary for 6R1G

• Entry DOI: 10.2210/pdb6r1g/pdb
• Descriptor: Outer surface 22 kDa lipoprotein, ZINC ION, TRIETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: periplasmic lipoprotein, lyme disease, membrane protein
• Biological source: Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
• Total number of polymer chains: 2
• Total formula weight: 39092.42

Authors

Brangulis, K.,Akopjana, I.,Petrovskis, I.,Kazaks, A.,Tars, K. (deposition date: 2019-03-14, release date: 2019-09-18, Last modification date: 2024-05-15)

Primary citation

Brangulis, K.,Akopjana, I.,Petrovskis, I.,Kazaks, A.,Jekabsons, A.,Jaudzems, K.,Viksna, A.,Bertins, M.,Tars, K.
Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.
Febs Lett., 594:317-326, 2020

PubMed Abstract: The periplasmic lipoprotein BB0365 of the Lyme disease agent Borrelia 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 Zn by the His51, His55, His140 residues, and the Zn -binding site indicates that BB0365 could act as a potential metalloenzyme; therefore, this structure narrows down the potential functions of BB0365, an essential protein for B. burgdorferi to cause Lyme disease.

PubMed: 31486526
DOI: 10.1002/1873-3468.13594

Experimental method

X-RAY DIFFRACTION (1.55 Å)