3ETX

Crystal structure of bacterial adhesin FadA L14A mutant

「2BC6」から置き換えられました

3ETX の概要

• エントリーDOI: 10.2210/pdb3etx/pdb
• 関連するPDBエントリー: 3ETW 3ETY 3ETZ
• 分子名称: Adhesin A (2 entities in total)
• 機能のキーワード: antiparallel helix-loop-helix, fada l14a mutant, cell adhesin, cell adhesion
• 由来する生物種: Fusobacterium nucleatum
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 40883.28

構造登録者

Nithianantham, S.,Xu, M.,Wu, N.,Shoham, M.,Han, Y.W. (登録日: 2008-10-08, 公開日: 2008-12-02, 最終更新日: 2023-09-06)

主引用文献

Nithianantham, S.,Xu, M.,Yamada, M.,Ikegami, A.,Shoham, M.,Han, Y.W.
Crystal Structure of FadA Adhesin from Fusobacterium nucleatum Reveals a Novel Oligomerization Motif, the Leucine Chain.
J.Biol.Chem., 284:3865-3872, 2009

PubMed Abstract: Many bacterial appendages have filamentous structures, often composed of repeating monomers assembled in a head-to-tail manner. The mechanisms of such linkages vary. We report here a novel protein oligomerization motif identified in the FadA adhesin from the Gram-negative bacterium Fusobacterium nucleatum. The 2.0 angstroms crystal structure of the secreted form of FadA (mFadA) reveals two antiparallel alpha-helices connected by an intervening 8-residue hairpin loop. Leucine-leucine contacts play a prominent dual intra- and intermolecular role in the structure and function of FadA. First, they comprise the main association between the two helical arms of the monomer; second, they mediate the head-to-tail association of monomers to form the elongated polymers. This leucine-mediated filamentous assembly of FadA molecules constitutes a novel structural motif termed the "leucine chain." The essential role of these residues in FadA is corroborated by mutagenesis of selected leucine residues, which leads to the abrogation of oligomerization, filament formation, and binding to host cells.

PubMed: 18996848
DOI: 10.1074/jbc.M805503200

実験手法

X-RAY DIFFRACTION (3 Å)