4KH3

Structure of a bacterial self-associating protein

4KH3 の概要

• エントリーDOI: 10.2210/pdb4kh3/pdb
• 関連するPDBエントリー: 1DAB 3H09
• 分子名称: Antigen 43, MALONATE ION (3 entities in total)
• 機能のキーワード: self-associating protein, uropathogenic escherichia coli, aida-i type autotransporter, ag43, aggregation, biofilm, immune system
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 50883.56

構造登録者

Heras, B.,Gee, C.L.,Schembri, M.A.,Totsika, M. (登録日: 2013-04-30, 公開日: 2014-01-15, 最終更新日: 2024-03-20)

主引用文献

Heras, B.,Totsika, M.,Peters, K.M.,Paxman, J.J.,Gee, C.L.,Jarrott, R.J.,Perugini, M.A.,Whitten, A.E.,Schembri, M.A.
The antigen 43 structure reveals a molecular Velcro-like mechanism of autotransporter-mediated bacterial clumping.
Proc.Natl.Acad.Sci.USA, 111:457-462, 2014

PubMed Abstract: Aggregation and biofilm formation are critical mechanisms for bacterial resistance to host immune factors and antibiotics. Autotransporter (AT) proteins, which represent the largest group of outer-membrane and secreted proteins in Gram-negative bacteria, contribute significantly to these phenotypes. Despite their abundance and role in bacterial pathogenesis, most AT proteins have not been structurally characterized, and there is a paucity of detailed information with regard to their mode of action. Here we report the structure-function relationships of Antigen 43 (Ag43a), a prototypic self-associating AT protein from uropathogenic Escherichia coli. The functional domain of Ag43a displays a twisted L-shaped β-helical structure firmly stabilized by a 3D hydrogen-bonded scaffold. Notably, the distinctive Ag43a L shape facilitates self-association and cell aggregation. Combining all our data, we define a molecular "Velcro-like" mechanism of AT-mediated bacterial clumping, which can be tailored to fit different bacterial lifestyles such as the formation of biofilms.

PubMed: 24335802
DOI: 10.1073/pnas.1311592111

実験手法

X-RAY DIFFRACTION (2.5 Å)