3UAU

Crystal structure of the lipoprotein JlpA

3UAU の概要

• エントリーDOI: 10.2210/pdb3uau/pdb
• 分子名称: Surface-exposed lipoprotein (1 entity in total)
• 機能のキーワード: adhesin, bacterial cell surface, cell adhesion
• 由来する生物種: Campylobacter jejuni subsp. jejuni
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 86768.48

構造登録者

Kawai, F.,Yeo, H.J. (登録日: 2011-10-22, 公開日: 2012-07-25, 最終更新日: 2024-10-16)

主引用文献

Kawai, F.,Paek, S.,Choi, K.J.,Prouty, M.,Kanipes, M.I.,Guerry, P.,Yeo, H.J.
Crystal structure of JlpA, a surface-exposed lipoprotein adhesin of Campylobacter jejuni.
J.Struct.Biol., 177:583-588, 2012

PubMed Abstract: The Campylobacter jejuni JlpA protein is a surface-exposed lipoprotein that was discovered as an adhesin promoting interaction with host epithelium cells, an early critical step in the pathogenesis of C. jejuni disease. Increasing evidence ascertained that JlpA is antigenic, indicating a role of JlpA in immune response during the infectious process. Here, we report the crystal structure of JlpA at 2.7Å resolution, revealing a catcher's mitt shaped unclosed half β-barrel. Although the apparent architecture of JlpA is somewhat reminiscent of other bacterial lipoproteins such as LolB, the topology of JlpA is unique among the bacterial surface proteins reported to date and therefore JlpA represents a novel bacterial cell surface lipoprotein. The concave face of the structure results in an unusually large hydrophobic basin with a localized acidic pocket, suggesting a possibility that JlpA may accommodate multiple ligands. Therefore, the structure provides framework for determining the molecular function of JlpA and new strategies for the rational design of small molecule inhibitors efficiently targeting JlpA.

PubMed: 22245776
DOI: 10.1016/j.jsb.2012.01.001

実験手法

X-RAY DIFFRACTION (2.7 Å)