8ONC

Structure of the C-terminal beta helix domain of the Bdellovibrio bacteriovorus Bd3182 fibre

8ONC の概要

• エントリーDOI: 10.2210/pdb8onc/pdb
• 分子名称: Cell wall surface anchor family protein, 1,2-ETHANEDIOL (3 entities in total)
• 機能のキーワード: fibre, adhesin, cell adhesion
• 由来する生物種: Bdellovibrio bacteriovorus HD100
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 93176.39

構造登録者

Caulton, S.G.,Lovering, A.L. (登録日: 2023-04-01, 公開日: 2023-10-25, 最終更新日: 2024-06-26)

主引用文献

Caulton, S.G.,Lambert, C.,Tyson, J.,Radford, P.,Al-Bayati, A.,Greenwood, S.,Banks, E.J.,Clark, C.,Till, R.,Pires, E.,Sockett, R.E.,Lovering, A.L.
Bdellovibrio bacteriovorus uses chimeric fibre proteins to recognize and invade a broad range of bacterial hosts.
Nat Microbiol, 9:214-227, 2024

PubMed Abstract: Predatory bacteria, like the model endoperiplasmic bacterium Bdellovibrio bacteriovorus, show several adaptations relevant to their requirements for locating, entering and killing other bacteria. The mechanisms underlying prey recognition and handling remain obscure. Here we use complementary genetic, microscopic and structural methods to address this deficit. During invasion, the B. bacteriovorus protein CpoB concentrates into a vesicular compartment that is deposited into the prey periplasm. Proteomic and structural analyses of vesicle contents reveal several fibre-like proteins, which we name the mosaic adhesive trimer (MAT) superfamily, and show localization on the predator surface before prey encounter. These dynamic proteins indicate a variety of binding capabilities, and we confirm that one MAT member shows specificity for surface glycans from a particular prey. Our study shows that the B. bacteriovorus MAT protein repertoire enables a broad means for the recognition and handling of diverse prey epitopes encountered during bacterial predation and invasion.

PubMed: 38177296
DOI: 10.1038/s41564-023-01552-2

実験手法

X-RAY DIFFRACTION (2 Å)