4J38
Structure of Borrelia burgdorferi Outer surface protein E in complex with Factor H domains 19-20
Summary for 4J38
| Entry DOI | 10.2210/pdb4j38/pdb |
| Related | 2G7I 2M4F 2XQW 3KXV 3KZJ |
| Descriptor | Outer surface protein E, Complement factor H, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | beta barrel, immune evasion, complement regulator binding, fh binding, membrane, immune system, erp paralog, lyme disease, bbcrasp-3 |
| Biological source | Borrelia burgdorferi More |
| Cellular location | Secreted: P08603 |
| Total number of polymer chains | 2 |
| Total formula weight | 31652.71 |
| Authors | Bhattacharjee, A.,Kolodziejczyk, R.,Kajander, T.,Goldman, A.,Jokiranta, T.S. (deposition date: 2013-02-05, release date: 2013-05-15, Last modification date: 2024-10-30) |
| Primary citation | Bhattacharjee, A.,Oeemig, J.S.,Kolodziejczyk, R.,Meri, T.,Kajander, T.,Lehtinen, M.J.,Iwai, H.,Jokiranta, T.S.,Goldman, A. Structural Basis for Complement Evasion by Lyme Disease Pathogen Borrelia burgdorferi J.Biol.Chem., 288:18685-18695, 2013 Cited by PubMed Abstract: Borrelia burgdorferi spirochetes that cause Lyme borreliosis survive for a long time in human serum because they successfully evade the complement system, an important arm of innate immunity. The outer surface protein E (OspE) of B. burgdorferi is needed for this because it recruits complement regulator factor H (FH) onto the bacterial surface to evade complement-mediated cell lysis. To understand this process at the molecular level, we used a structural approach. First, we solved the solution structure of OspE by NMR, revealing a fold that has not been seen before in proteins involved in complement regulation. Next, we solved the x-ray structure of the complex between OspE and the FH C-terminal domains 19 and 20 (FH19-20) at 2.83 Å resolution. The structure shows that OspE binds FH19-20 in a way similar to, but not identical with, that used by endothelial cells to bind FH via glycosaminoglycans. The observed interaction of OspE with FH19-20 allows the full function of FH in down-regulation of complement activation on the bacteria. This reveals the molecular basis for how B. burgdorferi evades innate immunity and suggests how OspE could be used as a potential vaccine antigen. PubMed: 23658013DOI: 10.1074/jbc.M113.459040 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.83 Å) |
Structure validation
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