2GR7

Hia 992-1098

2GR7 の概要

• エントリーDOI: 10.2210/pdb2gr7/pdb
• 関連するPDBエントリー: 2GR8
• 分子名称: Adhesin, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (3 entities in total)
• 機能のキーワード: trimeric autotransporter, adhesion, membrane protein, protein secretion, microbial pathogenesis
• 由来する生物種: Haemophilus influenzae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 78748.37

構造登録者

Meng, G.,Waksman, G. (登録日: 2006-04-23, 公開日: 2006-05-23, 最終更新日: 2024-02-14)

主引用文献

Meng, G.,Surana, N.K.,St Geme III, J.W.,Waksman, G.
Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter.
Embo J., 25:2297-2304, 2006

PubMed Abstract: Autotransporter proteins are defined by the ability to drive their own secretion across the bacterial outer membrane. The Hia autotransporter of Haemophilus influenzae belongs to the trimeric autotransporter subfamily and mediates bacterial adhesion to the respiratory epithelium. In this report, we present the crystal structure of the C-terminal end of Hia, corresponding to the entire Hia translocator domain and part of the passenger domain (residues 992-1098). This domain forms a beta-barrel with 12 transmembrane beta-strands, including four strands from each subunit. The beta-barrel has a central channel of 1.8 nm in diameter that is traversed by three N-terminal alpha-helices, one from each subunit. Mutagenesis studies demonstrate that the transmembrane portion of the three alpha-helices and the loop region between the alpha-helices and the neighboring beta-strands are essential for stability of the trimeric structure of the translocator domain, and that trimerization of the translocator domain is a prerequisite for translocator activity. Overall, this study provides important insights into the mechanism of translocation in trimeric autotransporters.

PubMed: 16688217
DOI: 10.1038/sj.emboj.7601132

実験手法

X-RAY DIFFRACTION (2.3 Å)