6fue: Difference between revisions
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The | ==Periplasmic coiled coil domain of the FapF amyloid transporter== | ||
<StructureSection load='6fue' size='340' side='right'caption='[[6fue]], [[Resolution|resolution]] 1.78Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6fue]] is a 6 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=6FUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FUE 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]] 1.78Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=6fue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fue OCA], [https://pdbe.org/6fue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fue RCSB], [https://www.ebi.ac.uk/pdbsum/6fue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fue 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, the fibres of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialised 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 A resolution. This domain forms a novel asymmetric trimeric coiled-coil that possesses a single buried tyrosine residue as well as a 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. | |||
The FapF amyloid secretion transporter possesses an atypical asymmetric coiled coil.,Rouse SL, Stylianou F, Grace Wu HY, Berry JL, Sewell L, Morgan RML, Sauerwein AC, Matthews S J Mol Biol. 2018 Jun 7. pii: S0022-2836(18)30583-7. doi:, 10.1016/j.jmb.2018.06.007. PMID:29886016<ref>PMID:29886016</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6fue" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Pseudomonas sp. UK4]] | |||
[[Category: Matthews SJ]] | |||
[[Category: Morgan RML]] | |||
[[Category: Rouse SL]] | |||
[[Category: Stylianou F]] | |||
Latest revision as of 15:31, 9 May 2024
Periplasmic coiled coil domain of the FapF amyloid transporterPeriplasmic coiled coil domain of the FapF amyloid transporter
Structural highlights
FunctionPublication Abstract from PubMedGram-negative bacteria possess specialised biogenesis machineries that facilitate the export of amyloid subunits, the fibres of which are key components of their biofilm matrix. The secretion of bacterial functional amyloid requires a specialised 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 A resolution. This domain forms a novel asymmetric trimeric coiled-coil that possesses a single buried tyrosine residue as well as a 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. The FapF amyloid secretion transporter possesses an atypical asymmetric coiled coil.,Rouse SL, Stylianou F, Grace Wu HY, Berry JL, Sewell L, Morgan RML, Sauerwein AC, Matthews S J Mol Biol. 2018 Jun 7. pii: S0022-2836(18)30583-7. doi:, 10.1016/j.jmb.2018.06.007. PMID:29886016[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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