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6SHU

Borrelia burgdorferi BmpD nucleoside binding protein bound to adenosine

Summary for 6SHU
Entry DOI10.2210/pdb6shu/pdb
DescriptorBasic membrane protein D, ADENOSINE, CHLORIDE ION, ... (5 entities in total)
Functional Keywordstransporter, nucleoside, purine, transport protein
Biological sourceBorrelia burgdorferi (strain JD1)
Total number of polymer chains1
Total formula weight39617.91
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 citationCuellar, 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: 31988175
DOI: 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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