6qbi

Publication Abstract from PubMed

Lyme disease is the most widespread vector-transmitted disease in North America and Europe, caused by infection with Borrelia burgdorferi sensu lato complex spirochetes. We report the solution NMR structure of the B. burgdorferi outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five alpha-helices and an extended C-terminal loop. The fold is similar to that of Borrelia turicatae outer surface protein BTA121, which is known to bind lipids. These results contribute to the understanding of Lyme disease pathogenesis by revealing the molecular structure of a protein from the widely found mlp family.

Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family.,Fridmanis J, Otikovs M, Brangulis K, Tars K, Jaudzems K Proteins. 2021 May;89(5):588-594. doi: 10.1002/prot.26011. Epub 2020 Sep 28. PMID:32949018^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.