4PZ5

Crystal structure of the second and third fibronectin F1 modules in complex with a fragment of BBK32 from Borrelia burgdorferi

4PZ5 の概要

• エントリーDOI: 10.2210/pdb4pz5/pdb
• 分子名称: Fibronectin, Fibronectin-binding protein BBK32 (3 entities in total)
• 機能のキーワード: fibronectin type one, cell adhesion, bacterial adhesion, fibronectin binding, extracellular matrix, plasma
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 11982.21

構造登録者

Harris, G.,Potts, J.R. (登録日: 2014-03-28, 公開日: 2014-07-02, 最終更新日: 2024-10-16)

主引用文献

Harris, G.,Ma, W.,Maurer, L.M.,Potts, J.R.,Mosher, D.F.
Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational Extension.
J.Biol.Chem., 289:22490-22499, 2014

PubMed Abstract: BBK32 is a fibronectin (FN)-binding protein expressed on the cell surface of Borrelia burgdorferi, the causative agent of Lyme disease. There is conflicting information about where and how BBK32 interacts with FN. We have characterized interactions of a recombinant 86-mer polypeptide, "Bbk32," comprising the unstructured FN-binding region of BBK32. Competitive enzyme-linked assays utilizing various FN fragments and epitope-mapped anti-FN monoclonal antibodies showed that Bbk32 binding involves both the fibrin-binding and the gelatin-binding domains of the 70-kDa N-terminal region (FN70K). Crystallographic and NMR analyses of smaller Bbk32 peptides complexed, respectively, with (2-3)FNI and (8-9)FNI, demonstrated that binding occurs by β-strand addition. Isothermal titration calorimetry indicated that Bbk32 binds to isolated FN70K more tightly than to intact FN. In a competitive enzyme-linked binding assay, complex formation with Bbk32 enhanced binding of FN with mAbIII-10 to the (10)FNIII module. Thus, Bbk32 binds to multiple FN type 1 modules of the FN70K region by a tandem β-zipper mechanism, and in doing so increases accessibility of FNIII modules that interact with other ligands. The similarity in the FN-binding mechanism of BBK32 and previously studied streptococcal proteins suggests that the binding and associated conformational change of FN play a role in infection.

PubMed: 24962582
DOI: 10.1074/jbc.M114.578419

実験手法

X-RAY DIFFRACTION (1.96 Å)