Description:
<jats:title>Abstract</jats:title><jats:p>Lyme disease is the most widespread vector‐transmitted disease in North America and Europe, caused by infection with <jats:italic>Borrelia burgdorferi sensu lato</jats:italic> complex spirochetes. We report the solution NMR structure of the <jats:italic>B. burgdorferi</jats:italic> outer surface lipoprotein BBP28, a member of the multicopy lipoprotein (mlp) family. The structure comprises a tether peptide, five α‐helices and an extended C‐terminal loop. The fold is similar to that of <jats:italic>Borrelia turicatae</jats:italic> 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.</jats:p>