6SHU
Borrelia burgdorferi BmpD nucleoside binding protein bound to adenosine
Summary for 6SHU
| Entry DOI | 10.2210/pdb6shu/pdb |
| Descriptor | Basic membrane protein D, ADENOSINE, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | transporter, nucleoside, purine, transport protein |
| Biological source | Borrelia burgdorferi (strain JD1) |
| Total number of polymer chains | 1 |
| Total formula weight | 39617.91 |
| Authors | Guedez, G.,Astrand, M.,Cuellar, J.,Hytonen, J.,Salminen, T.A. (deposition date: 2019-08-08, release date: 2020-02-12, Last modification date: 2024-05-15) |
| Primary citation | Cuellar, J.,Astrand, M.,Elovaara, H.,Pietikainen, A.,Siren, S.,Liljeblad, A.,Guedez, G.,Salminen, T.A.,Hytonen, J. Structural and Biomolecular Analyses of Borrelia burgdorferi BmpD Reveal a Substrate-Binding Protein of an ABC-Type Nucleoside Transporter Family. Infect.Immun., 88:-, 2020 Cited by PubMed Abstract: , the causative agent of tick-borne Lyme borreliosis (LB), has a limited metabolic capacity and needs to acquire nutrients, such as amino acids, fatty acids, and nucleic acids, from the host environment. Using X-ray crystallography, liquid chromatography-mass spectrometry, microscale thermophoresis, and cellular localization studies, we show that basic membrane protein D (BmpD) is a periplasmic substrate-binding protein of an ABC transporter system binding to purine nucleosides. Nucleosides are essential for bacterial survival in the host organism, and these studies suggest a key role for BmpD in the purine salvage pathway of Because lacks the enzymes required for purine synthesis, BmpD may play a vital role in ensuring access to the purines needed to sustain an infection in the host. Furthermore, we show that, although human LB patients develop anti-BmpD antibodies, immunization of mice with BmpD does not confer protection against infection. PubMed: 31988175DOI: 10.1128/IAI.00962-19 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.43002869382 Å) |
Structure validation
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