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PDBsum entry 5o68
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Membrane protein
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PDB id
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5o68
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Contents |
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272 a.a.
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(+ 2 more)
274 a.a.
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254 a.a.
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256 a.a.
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PDB id:
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| Name: |
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Membrane protein
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Title:
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Crystal structure of the pseudomonas functional amyloid secretion protein fapf - r157a mutant
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Structure:
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Fapf. Chain: a, b, c, d, e, f, g, h, i, j, k, l. Engineered: yes. Mutation: yes
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Source:
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Pseudomonas sp. Uk4. Organism_taxid: 452680. Gene: fapf, psuk4_00060. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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3.08Å
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R-factor:
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0.322
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R-free:
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0.370
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Authors:
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S.L.Rouse,S.Hare,S.Lambert,R.M.L.Morgan,W.J.Hawthorne,J.Berry, S.J.Matthews
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Key ref:
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S.L.Rouse
et al.
(2017).
A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.
Nat Commun,
8,
263.
PubMed id:
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Date:
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05-Jun-17
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Release date:
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23-Aug-17
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PROCHECK
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Headers
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References
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C4IN73
(C4IN73_9PSED) -
FapF from Pseudomonas sp. UK4
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Seq:
Struc:
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430 a.a.
272 a.a.*
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C4IN73
(C4IN73_9PSED) -
FapF from Pseudomonas sp. UK4
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Seq:
Struc:
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430 a.a.
274 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F, G, H, I, J, K, L:
E.C.?
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Nat Commun
8:263
(2017)
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PubMed id:
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A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.
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S.L.Rouse,
W.J.Hawthorne,
J.L.Berry,
D.S.Chorev,
S.A.Ionescu,
S.Lambert,
F.Stylianou,
W.Ewert,
U.Mackie,
R.M.L.Morgan,
D.Otzen,
F.A.Herbst,
P.H.Nielsen,
M.Dueholm,
H.Bayley,
C.V.Robinson,
S.Hare,
S.Matthews.
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ABSTRACT
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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.
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