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The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil

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...

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Detalles Bibliográficos
Autores principales: Rouse, Sarah L., Stylianou, Fisentzos, Wu, H.Y. Grace, Berry, Jamie-Lee, Sewell, Lee, Morgan, R. Marc L., Sauerwein, Andrea C., Matthews, Steve
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6173795/
https://www.ncbi.nlm.nih.gov/pubmed/29886016
http://dx.doi.org/10.1016/j.jmb.2018.06.007
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author Rouse, Sarah L.
Stylianou, Fisentzos
Wu, H.Y. Grace
Berry, Jamie-Lee
Sewell, Lee
Morgan, R. Marc L.
Sauerwein, Andrea C.
Matthews, Steve
author_facet Rouse, Sarah L.
Stylianou, Fisentzos
Wu, H.Y. Grace
Berry, Jamie-Lee
Sewell, Lee
Morgan, R. Marc L.
Sauerwein, Andrea C.
Matthews, Steve
author_sort Rouse, Sarah L.
collection PubMed
description 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.
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spelling pubmed-61737952018-10-12 The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil Rouse, Sarah L. Stylianou, Fisentzos Wu, H.Y. Grace Berry, Jamie-Lee Sewell, Lee Morgan, R. Marc L. Sauerwein, Andrea C. Matthews, Steve J Mol Biol Article 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. Elsevier 2018-10-12 /pmc/articles/PMC6173795/ /pubmed/29886016 http://dx.doi.org/10.1016/j.jmb.2018.06.007 Text en © 2018 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Rouse, Sarah L.
Stylianou, Fisentzos
Wu, H.Y. Grace
Berry, Jamie-Lee
Sewell, Lee
Morgan, R. Marc L.
Sauerwein, Andrea C.
Matthews, Steve
The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title_full The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title_fullStr The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title_full_unstemmed The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title_short The FapF Amyloid Secretion Transporter Possesses an Atypical Asymmetric Coiled Coil
title_sort fapf amyloid secretion transporter possesses an atypical asymmetric coiled coil
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6173795/
https://www.ncbi.nlm.nih.gov/pubmed/29886016
http://dx.doi.org/10.1016/j.jmb.2018.06.007
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