Imperial College London
Alternate

Prof Steve Matthews

Faculty of Natural Sciences, Department of Life Sciences

Professor of Chemical and Structural Biology
 
 
 
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Contact

 

+44 (0)20 7594 5315s.j.matthews Website

 
 
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Location

 

602Sir Ernst Chain BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Rouse:2018:10.1016/j.jmb.2018.06.007,
author = {Rouse, S and Stylianou, F and wu, G and Berry, J and Sewell, L and Morgan, M and Sauerwein, AC and Matthews, S},
doi = {10.1016/j.jmb.2018.06.007},
journal = {Journal of Molecular Biology},
pages = {3863--3871},
title = {The FapF amyloid secretion transporter possesses an atypical asymmetric coiled coil},
url = {http://dx.doi.org/10.1016/j.jmb.2018.06.007},
volume = {430},
year = {2018}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - 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.
AU  - Rouse,S
AU  - Stylianou,F
AU  - wu,G
AU  - Berry,J
AU  - Sewell,L
AU  - Morgan,M
AU  - Sauerwein,AC
AU  - Matthews,S
DO  - 10.1016/j.jmb.2018.06.007
EP  - 3871
PY  - 2018///
SN  - 0022-2836
SP  - 3863
TI  - The FapF amyloid secretion transporter possesses an atypical asymmetric coiled coil
T2  - Journal of Molecular Biology
UR  - http://dx.doi.org/10.1016/j.jmb.2018.06.007
UR  - https://www.sciencedirect.com/science/article/pii/S0022283618305837?via%3Dihub
UR  - http://hdl.handle.net/10044/1/61043
VL  - 430
ER  -
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