6r1g

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

spinqualitylabelsall models 6r1g, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6r1g is a 2 chain structure with sequence from Borbu. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PG4, PGE, ZN Gene: p22, BB_0365 (BORBU) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed 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(2+) by the His51, His55, His140 residues, and the Zn(2+) -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. Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.,Brangulis K, Akopjana I, Petrovskis I, Kazaks A, Jekabsons A, Jaudzems K, Viksna A, Bertins M, Tars K FEBS Lett. 2020 Jan;594(2):317-326. doi: 10.1002/1873-3468.13594. Epub 2019 Sep, 13. PMID:31486526 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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