6FUE

Periplasmic coiled coil domain of the FapF amyloid transporter

Summary for 6FUE

• Entry DOI: 10.2210/pdb6fue/pdb
• Descriptor: FapF, ZINC ION, SODIUM ION, ... (5 entities in total)
• Functional Keywords: trimeric periplasmic coiled coil, protein transport
• Biological source: Pseudomonas sp. UK4
• Total number of polymer chains: 6
• Total formula weight: 28278.27

Authors

Rouse, S.L.,Stylianou, F.,Morgan, R.M.L.,Matthews, S.J. (deposition date: 2018-02-26, release date: 2018-06-20, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.78 Å)