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2XWX

Vibrio cholerae colonization factor GbpA crystal structure

2XWX の概要
エントリーDOI10.2210/pdb2xwx/pdb
分子名称GLCNAC-BINDING PROTEIN A (2 entities in total)
機能のキーワードchitin-binding protein
由来する生物種VIBRIO CHOLERAE
細胞内の位置Secreted : Q9KLD5
タンパク質・核酸の鎖数2
化学式量合計86585.97
構造登録者
主引用文献Wong, E.,Vaaje-Kolstad, G.,Ghosh, A.,Hurtado-Guerrero, R.,Konarev, P.V.,Ibrahim, A.F.M.,Svergun, D.I.,Eijsink, V.G.H.,Chatterjee, N.S.,Van Aalten, D.M.F.
The Vibrio Cholerae Colonization Factor Gbpa Possesses a Modular Structure that Governs Binding to Different Host Surfaces.
Plos Pathog., 8:2373-, 2012
Cited by
PubMed Abstract: Vibrio cholerae is a bacterial pathogen that colonizes the chitinous exoskeleton of zooplankton as well as the human gastrointestinal tract. Colonization of these different niches involves an N-acetylglucosamine binding protein (GbpA) that has been reported to mediate bacterial attachment to both marine chitin and mammalian intestinal mucin through an unknown molecular mechanism. We report structural studies that reveal that GbpA possesses an unusual, elongated, four-domain structure, with domains 1 and 4 showing structural homology to chitin binding domains. A glycan screen revealed that GbpA binds to GlcNAc oligosaccharides. Structure-guided GbpA truncation mutants show that domains 1 and 4 of GbpA interact with chitin in vitro, whereas in vivo complementation studies reveal that domain 1 is also crucial for mucin binding and intestinal colonization. Bacterial binding studies show that domains 2 and 3 bind to the V. cholerae surface. Finally, mouse virulence assays show that only the first three domains of GbpA are required for colonization. These results explain how GbpA provides structural/functional modular interactions between V. cholerae, intestinal epithelium and chitinous exoskeletons.
PubMed: 22253590
DOI: 10.1371/JOURNAL.PPAT.1002373
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.8 Å)
構造検証レポート
Validation report summary of 2xwx
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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