6BEA

Crystal structure of the autotransporter UpaB from E. coli strain CFT073

6BEA の概要

• エントリーDOI: 10.2210/pdb6bea/pdb
• 関連するPDBエントリー: 4KH3
• 分子名称: Autotransporter protein UpaB, GLYCEROL, HEXAETHYLENE GLYCOL, ... (8 entities in total)
• 機能のキーワード: autotransporter protein, bacterial adhesin, virulence factor, fibronectin, glycosaminoglycan, protein binding
• 由来する生物種: Escherichia coli O6:H1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 48668.76

構造登録者

Paxman, J.J.,Heras, B. (登録日: 2017-10-25, 公開日: 2019-04-10, 最終更新日: 2024-03-13)

主引用文献

Paxman, J.J.,Lo, A.W.,Sullivan, M.J.,Panjikar, S.,Kuiper, M.,Whitten, A.E.,Wang, G.,Luan, C.H.,Moriel, D.G.,Tan, L.,Peters, K.M.,Phan, M.D.,Gee, C.L.,Ulett, G.C.,Schembri, M.A.,Heras, B.
Unique structural features of a bacterial autotransporter adhesin suggest mechanisms for interaction with host macromolecules.
Nat Commun, 10:1967-1967, 2019

PubMed Abstract: Autotransporters are the largest family of outer membrane and secreted proteins in Gram-negative bacteria. Most autotransporters are localised to the bacterial surface where they promote colonisation of host epithelial surfaces. Here we present the crystal structure of UpaB, an autotransporter that is known to contribute to uropathogenic E. coli (UPEC) colonisation of the urinary tract. We provide evidence that UpaB can interact with glycosaminoglycans and host fibronectin. Unique modifications to its core β-helical structure create a groove on one side of the protein for interaction with glycosaminoglycans, while the opposite face can bind fibronectin. Our findings reveal far greater diversity in the autotransporter β-helix than previously thought, and suggest that this domain can interact with host macromolecules. The relevance of these interactions during infection remains unclear.

PubMed: 31036849
DOI: 10.1038/s41467-019-09814-6

実験手法

X-RAY DIFFRACTION (1.97 Å)