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Publication Abstract from PubMed

Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits, the fibres of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialised 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 A resolution. This domain forms a novel asymmetric trimeric coiled-coil that possesses a single buried tyrosine residue as well as a 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.

The FapF amyloid secretion transporter possesses an atypical asymmetric coiled coil.,Rouse SL, Stylianou F, Grace Wu HY, Berry JL, Sewell L, Morgan RML, Sauerwein AC, Matthews S J Mol Biol. 2018 Jun 7. pii: S0022-2836(18)30583-7. doi:, 10.1016/j.jmb.2018.06.007. PMID:29886016^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.