View source for 5o65


==Crystal Structure of the Pseudomonas functional amyloid secretion protein FapF==
<StructureSection load='5o65' size='340' side='right'caption='[[5o65]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5o65]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_sp._UK4 Pseudomonas sp. UK4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5O65 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5O65 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5o65 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5o65 OCA], [https://pdbe.org/5o65 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5o65 RCSB], [https://www.ebi.ac.uk/pdbsum/5o65 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5o65 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/C4IN73_9PSED C4IN73_9PSED] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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 beta-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.

A new class of hybrid secretion system is employed in Pseudomonas amyloid biogenesis.,Rouse SL, Hawthorne WJ, Berry JL, Chorev DS, Ionescu SA, Lambert S, Stylianou F, Ewert W, Mackie U, Morgan RML, Otzen D, Herbst FA, Nielsen PH, Dueholm M, Bayley H, Robinson CV, Hare S, Matthews S Nat Commun. 2017 Aug 15;8(1):263. doi: 10.1038/s41467-017-00361-6. PMID:28811582<ref>PMID:28811582</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5o65" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas sp. UK4]]
[[Category: Berry J]]
[[Category: Hare S]]
[[Category: Hawthorne WJ]]
[[Category: Lambert S]]
[[Category: Matthews SJ]]
[[Category: Morgan RML]]
[[Category: Rouse SL]]