6fue | pdb_00006fue

Periplasmic coiled coil domain of the FapF amyloid transporter

spinqualitylabelsall models 6fue, resolution 1.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6fue is a 6 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: IPA, NA, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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