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RESEARCH PRODUCT
Structural analysis of Borrelia burgdorferi periplasmic lipoprotein BB0365 involved in Lyme disease infection.
Ivars PetrovskisAndris KazaksKristaps JaudzemsKaspars TarsKaspars TarsArturs ViksnaKalvis BrangulisInara AkopjanaAtis JekabsonsMaris Bertinssubject
Protein FoldingProtein ConformationLipoproteinsBiophysicsBiochemistryMicrobiology03 medical and health sciencesLyme diseaseBacterial ProteinsStructural BiologyOxidoreductaseGeneticsmedicineHumansBinding siteBorrelia burgdorferiMolecular BiologyFerredoxin030304 developmental biologychemistry.chemical_classification0303 health sciencesLyme DiseaseBinding SitesbiologyChemistry030302 biochemistry & molecular biologyCell BiologyPeriplasmic spacebacterial infections and mycosesmedicine.diseasebiology.organism_classificationZincMembrane proteinBorrelia burgdorferiPeriplasmbacteriaNAD+ kinaseSodium-Potassium-Exchanging ATPasedescription
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 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 for B. burgdorferi to cause Lyme disease.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-05-28 | FEBS lettersReferences |