View source for 6e14


==Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD==
<SX load='6e14' size='340' side='right' viewer='molstar' caption='[[6e14]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6e14]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E14 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E14 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</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=6e14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e14 OCA], [https://pdbe.org/6e14 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e14 RCSB], [https://www.ebi.ac.uk/pdbsum/6e14 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e14 ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/FIMD_ECOLI FIMD_ECOLI] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
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== Publication Abstract from PubMed ==
Pathogenic bacteria such as Escherichia coli assemble surface structures termed pili, or fimbriae, to mediate binding to host-cell receptors(1). Type 1 pili are assembled via the conserved chaperone-usher pathway(2-5). The outer-membrane usher FimD recruits pilus subunits bound by the chaperone FimC via the periplasmic N-terminal domain of the usher. Subunit translocation through the beta-barrel channel of the usher occurs at the two C-terminal domains (which we label CTD1 and CTD2) of this protein. How the chaperone-subunit complex bound to the N-terminal domain is handed over to the C-terminal domains, as well as the timing of subunit polymerization into the growing pilus, have previously been unclear. Here we use cryo-electron microscopy to capture a pilus assembly intermediate (FimD-FimC-FimF-FimG-FimH) in a conformation in which FimD is in the process of handing over the chaperone-bound end of the growing pilus to the C-terminal domains. In this structure, FimF has already polymerized with FimG, and the N-terminal domain of FimD swings over to bind CTD2; the N-terminal domain maintains contact with FimC-FimF, while at the same time permitting access to the C-terminal domains. FimD has an intrinsically disordered N-terminal tail that precedes the N-terminal domain. This N-terminal tail folds into a helical motif upon recruiting the FimC-subunit complex, but reorganizes into a loop to bind CTD2 during handover. Because both the N-terminal and C-terminal domains of FimD are bound to the end of the growing pilus, the structure further suggests a mechanism for stabilizing the assembly intermediate to prevent the pilus fibre diffusing away during the incorporation of thousands of subunits.

Handover mechanism of the growing pilus by the bacterial outer-membrane usher FimD.,Du M, Yuan Z, Yu H, Henderson N, Sarowar S, Zhao G, Werneburg GT, Thanassi DG, Li H Nature. 2018 Oct 3. pii: 10.1038/s41586-018-0587-z. doi:, 10.1038/s41586-018-0587-z. PMID:30283140<ref>PMID:30283140</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 6e14" style="background-color:#fffaf0;"></div>

==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Du M]]
[[Category: Henderson N]]
[[Category: Li H]]
[[Category: Sarowar S]]
[[Category: Thanassi DG]]
[[Category: Werneburg GT]]
[[Category: Yu H]]
[[Category: Yuan Z]]
[[Category: Zhao G]]