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6SHU

Borrelia burgdorferi BmpD nucleoside binding protein bound to adenosine

6SHU の概要
エントリーDOI10.2210/pdb6shu/pdb
分子名称Basic membrane protein D, ADENOSINE, CHLORIDE ION, ... (5 entities in total)
機能のキーワードtransporter, nucleoside, purine, transport protein
由来する生物種Borrelia burgdorferi (strain JD1)
タンパク質・核酸の鎖数1
化学式量合計39617.91
構造登録者
Guedez, G.,Astrand, M.,Cuellar, J.,Hytonen, J.,Salminen, T.A. (登録日: 2019-08-08, 公開日: 2020-02-12, 最終更新日: 2024-05-15)
主引用文献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: 31988175
DOI: 10.1128/IAI.00962-19
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.43002869382 Å)
構造検証レポート
Validation report summary of 6shu
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-22に公開中

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