6QBI
NMR structure of BB_P28, Borrelia burgdorferi outer surface lipoprotein
Summary for 6QBI
| Entry DOI | 10.2210/pdb6qbi/pdb |
| NMR Information | BMRB: 34344 |
| Descriptor | Surface protein, mlp lipoprotein family (1 entity in total) |
| Functional Keywords | lipoprotein, membrane protein |
| Biological source | Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680) |
| Total number of polymer chains | 1 |
| Total formula weight | 11038.11 |
| Authors | Fridmanis, J.,Otikovs, M.,Brangulis, K.,Jaudzems, K. (deposition date: 2018-12-21, release date: 2020-01-29, Last modification date: 2024-11-06) |
| Primary citation | Fridmanis, J.,Otikovs, M.,Brangulis, K.,Tars, K.,Jaudzems, K. Solution NMR structure of Borrelia burgdorferi outer surface lipoprotein BBP28, a member of the mlp protein family. Proteins, 2020 Cited by PubMed Abstract: 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 α-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. PubMed: 32949018DOI: 10.1002/prot.26011 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
Download full validation report
