BibTex format

author = {rouse, S and hawthorne and berry and Chorev, D and Ionescu, S and Lambert, S and Stylianou, F and Ewert, W and Mackie, U and Morgan and Otzen, D and Herbst, F-A and Nielsen, P and Dueholm, M and Bayley, H and Robinson, C and Hare, S and Matthews, S},
doi = {10.1038/s41467-017-00361-6},
journal = {Nature Communications},
title = {A new class of hybrid secretion system is employed in 2 Pseudomonas amyloid biogenesis},
url = {},
volume = {8},
year = {2017}

RIS format (EndNote, RefMan)

AB - Gram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits for construction of a biofilm matrix. The secretion of bacterial functional amyloid requires a bespoke outer-membrane protein channel through which unfolded amyloid substrates are translocated. Here, we combine X-ray crystallography, native mass spectrometry, single-channel electrical recording, molecular simulations and circular dichroism measurements to provide high-resolution structural insight into the functional amyloid transporter from Pseudomonas, FapF. FapF forms a trimer of gated β-barrel channels in which opening is regulated by a helical plug connected to an extended coil-coiled platform spanning the bacterial periplasm. Although FapF represents a unique type of secretion system, it shares mechanistic features with a diverse range of peptide translocation systems. Our findings highlight alternative strategies for handling and export of amyloid protein sequences.
AU - rouse,S
AU - hawthorne
AU - berry
AU - Chorev,D
AU - Ionescu,S
AU - Lambert,S
AU - Stylianou,F
AU - Ewert,W
AU - Mackie,U
AU - Morgan
AU - Otzen,D
AU - Herbst,F-A
AU - Nielsen,P
AU - Dueholm,M
AU - Bayley,H
AU - Robinson,C
AU - Hare,S
AU - Matthews,S
DO - 10.1038/s41467-017-00361-6
PY - 2017///
SN - 2041-1723
TI - A new class of hybrid secretion system is employed in 2 Pseudomonas amyloid biogenesis
T2 - Nature Communications
UR -
UR -
VL - 8
ER -