6qbi | pdb_00006qbi

NMR structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein

spinqualitylabelsall models 6qbi Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6qbi is a 1 chain structure with sequence from Borreliella burgdorferi B31. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MLPA_BORBU An outer membrane protein that may participate in pathogenesis. Some human Lyme disease patients have antibodies against this protein (PubMed:10948116). The Mlp proteins probably undergo intragenic recombination, generating new alleles (Probable). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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