5O65

Crystal Structure of the Pseudomonas functional amyloid secretion protein FapF

Summary for 5O65

• Entry DOI: 10.2210/pdb5o65/pdb
• Related: 5o67 5o68
• Descriptor: FapF, LAURYL DIMETHYLAMINE-N-OXIDE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (5 entities in total)
• Functional Keywords: amyloid, secretion, plug, barrel, membrane protein
• Biological source: Pseudomonas sp. UK4
• Total number of polymer chains: 3
• Total formula weight: 113711.12

Authors

Rouse, S.L.,Hare, S.,Lambert, S.,Morgan, R.M.L.,Hawthorne, W.J.,Berry, J.,Matthews, S.J. (deposition date: 2017-06-05, release date: 2017-08-23, Last modification date: 2024-11-13)

Primary citation

Rouse, S.L.,Hawthorne, W.J.,Berry, J.L.,Chorev, D.S.,Ionescu, S.A.,Lambert, S.,Stylianou, F.,Ewert, W.,Mackie, U.,Morgan, R.M.L.,Otzen, D.,Herbst, F.A.,Nielsen, P.H.,Dueholm, M.,Bayley, H.,Robinson, C.V.,Hare, S.,Matthews, S.
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.
Nat Commun, 8:263-263, 2017

PubMed 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.Gram-negative bacteria assemble biofilms from amyloid fibres, which translocate across the outer membrane as unfolded amyloid precursors through a secretion system. Here, the authors characterise the structural details of the amyloid transporter FapF in Pseudomonas.

PubMed: 28811582
DOI: 10.1038/s41467-017-00361-6

Experimental method

X-RAY DIFFRACTION (2.5 Å)