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Instruments / Technical Area	Publication Details	Published	Actions
I03-Macromolecular Crystallography	A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis Sarah L. Rouse , William J. Hawthorne , Jamie-Lee Berry , Dror S. Chorev , Sandra A. Ionescu , Sebastian Lambert , Fisentzos Stylianou , Wiebke Ewert , Uma Mackie , R. Marc L. Morgan , Daniel Otzen , Florian-Alexander Herbst , Per H. Nielsen , Morten Dueholm , Hagan Bayley , Carol V. Robinson , Stephen Hare , Stephen Matthews Nature Communications 8 DOI: 10.1038/s41467-017-00361-6 Diamond Proposal Number(s): [12579] Open Access Show Abstract ▼ Abstract: 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.	Aug 2017

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I03-Macromolecular Crystallography

A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis