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3F6I

Structure of the SeMet labeled F4 fibrial chaperone FaeE

3F6I の概要
エントリーDOI10.2210/pdb3f6i/pdb
関連するPDBエントリー3F65 3F6L
分子名称Chaperone protein faeE (2 entities in total)
機能のキーワードimmunoglobulin-like fold, cell projection, chaperone, fimbrium, immunoglobulin domain, periplasm, plasmid
由来する生物種Escherichia coli
細胞内の位置Periplasm: P25401
タンパク質・核酸の鎖数2
化学式量合計49977.60
構造登録者
Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Wyns, L.,De Greve, H.,Bouckaert, J. (登録日: 2008-11-06, 公開日: 2009-05-19, 最終更新日: 2024-11-20)
主引用文献Van Molle, I.,Moonens, K.,Buts, L.,Garcia-Pino, A.,Panjikar, S.,Wyns, L.,De Greve, H.,Bouckaert, J.
The F4 fimbrial chaperone FaeE is stable as a monomer that does not require self-capping of its pilin-interactive surfaces
Acta Crystallogr.,Sect.D, 65:411-420, 2009
Cited by
PubMed Abstract: Many Gram-negative bacteria use the chaperone-usher pathway to express adhesive surface structures, such as fimbriae, in order to mediate attachment to host cells. Periplasmic chaperones are required to shuttle fimbrial subunits or pilins through the periplasmic space in an assembly-competent form. The chaperones cap the hydrophobic surface of the pilins through a donor-strand complementation mechanism. FaeE is the periplasmic chaperone required for the assembly of the F4 fimbriae of enterotoxigenic Escherichia coli. The FaeE crystal structure shows a dimer formed by interaction between the pilin-binding interfaces of the two monomers. Dimerization and tetramerization have been observed previously in crystal structures of fimbrial chaperones and have been suggested to serve as a self-capping mechanism that protects the pilin-interactive surfaces in solution in the absence of the pilins. However, thermodynamic and biochemical data show that FaeE occurs as a stable monomer in solution. Other lines of evidence indicate that self-capping of the pilin-interactive interfaces is not a mechanism that is conservedly applied by all periplasmic chaperones, but is rather a case-specific solution to cap aggregation-prone surfaces.
PubMed: 19390146
DOI: 10.1107/S0907444909005174
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.788 Å)
構造検証レポート
Validation report summary of 3f6i
検証レポート(詳細版)ダウンロードをダウンロード

246905

件を2025-12-31に公開中

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