6FUE

Periplasmic coiled coil domain of the FapF amyloid transporter

6FUE の概要

• エントリーDOI: 10.2210/pdb6fue/pdb
• 分子名称: FapF, ZINC ION, SODIUM ION, ... (5 entities in total)
• 機能のキーワード: trimeric periplasmic coiled coil, protein transport
• 由来する生物種: Pseudomonas sp. UK4
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 28278.27

構造登録者

Rouse, S.L.,Stylianou, F.,Morgan, R.M.L.,Matthews, S.J. (登録日: 2018-02-26, 公開日: 2018-06-20, 最終更新日: 2024-05-08)

主引用文献

Rouse, S.L.,Stylianou, F.,Wu, H.Y.G.,Berry, J.L.,Sewell, L.,Morgan, R.M.L.,Sauerwein, A.C.,Matthews, S.
The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil.
J. Mol. Biol., 430:3863-3871, 2018

PubMed Abstract: Gram-negative bacteria possess specialized biogenesis machineries that facilitate the export of amyloid subunits, the fibers of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialized outer-membrane protein channel through which unfolded amyloid substrates are translocated. We previously reported the crystal structure of the membrane-spanning domain of the amyloid subunit transporter FapF from Pseudomonas. However, the structure of the periplasmic domain, which is essential for amyloid transport, is yet to be determined. Here, we present the crystal structure of the N-terminal periplasmic domain at 1.8-Å resolution. This domain forms a novel asymmetric trimeric coiled coil that possesses a single buried tyrosine residue as well as an extensive hydrogen-bonding network within a glutamine layer. This new structural insight allows us to understand this newly described functional amyloid secretion system in greater detail.

PubMed: 29886016
DOI: 10.1016/j.jmb.2018.06.007

実験手法

X-RAY DIFFRACTION (1.78 Å)