1S7M

Crystal Structure of HiaBD1

1S7M の概要

• エントリーDOI: 10.2210/pdb1s7m/pdb
• 分子名称: Hia (2 entities in total)
• 機能のキーワード: adhesion, homotrimer, autotransporter, cell adhesion
• 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: 108135.80

構造登録者

Yeo, H.J.,Cotter, S.E.,Laarmann, S.,Juehne, T.,St Geme, J.W.,Waksman, G. (登録日: 2004-01-29, 公開日: 2004-04-06, 最終更新日: 2024-04-03)

主引用文献

Yeo, H.J.,Cotter, S.E.,Laarmann, S.,Juehne, T.,St Geme, J.W.,Waksman, G.
Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter.
Embo J., 23:1245-1256, 2004

PubMed Abstract: Haemophilus influenzae is an important human pathogen that initiates infection by colonizing the upper respiratory tract. The H. influenzae Hia autotransporter is an adhesive protein that promotes adherence to respiratory epithelial cells. Hia adhesive activity resides in two homologous binding domains, called HiaBD1 and HiaBD2. These domains interact with the same host cell receptor, but bind with different affinities. In this report, we describe the crystal structure of the high-affinity HiaBD1 binding domain, which has a novel trimeric architecture with three-fold symmetry and a mushroom shape. The subunit constituents of the trimer are extensively intertwined. The receptor-binding pocket is formed by an acidic patch that is present on all three faces of the trimer, providing potential for a multivalent interaction with the host cell surface, analogous to observations with the trimeric tumor necrosis factor superfamily of proteins. Hia is a novel example of a bacterial trimeric adhesin and may be the prototype member of a large family of bacterial virulence proteins with a similar architecture.

PubMed: 15029242
DOI: 10.1038/sj.emboj.7600142

実験手法

X-RAY DIFFRACTION (2.1 Å)