View source for 1zdx


==Solution Structure of the type 1 pilus assembly platform FimD(25-125)==
<StructureSection load='1zdx' size='340' side='right'caption='[[1zdx]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1zdx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZDX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZDX FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1zdx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zdx OCA], [https://pdbe.org/1zdx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zdx RCSB], [https://www.ebi.ac.uk/pdbsum/1zdx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zdx ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/FIMD_ECOLI FIMD_ECOLI] Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zd/1zdx_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1zdx ConSurf].
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== Publication Abstract from PubMed ==
Adhesive type 1 pili from uropathogenic Escherichia coli are filamentous protein complexes that are attached to the assembly platform FimD in the outer membrane. During pilus assembly, FimD binds complexes between the chaperone FimC and type 1 pilus subunits in the periplasm and mediates subunit translocation to the cell surface. Here we report nuclear magnetic resonance and X-ray protein structures of the N-terminal substrate recognition domain of FimD (FimD(N)) before and after binding of a chaperone-subunit complex. FimD(N) consists of a flexible N-terminal segment of 24 residues, a structured core with a novel fold, and a C-terminal hinge segment. In the ternary complex, residues 1-24 of FimD(N) specifically interact with both FimC and the subunit, acting as a sensor for loaded FimC molecules. Together with in vivo complementation studies, we show how this mechanism enables recognition and discrimination of different chaperone-subunit complexes by bacterial pilus assembly platforms.

Structural basis of chaperone-subunit complex recognition by the type 1 pilus assembly platform FimD.,Nishiyama M, Horst R, Eidam O, Herrmann T, Ignatov O, Vetsch M, Bettendorff P, Jelesarov I, Grutter MG, Wuthrich K, Glockshuber R, Capitani G EMBO J. 2005 Jun 15;24(12):2075-86. Epub 2005 May 26. PMID:15920478<ref>PMID:15920478</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 1zdx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Bettendorff P]]
[[Category: Capitani G]]
[[Category: Glockshuber R]]
[[Category: Grutter M]]
[[Category: Herrmann T]]
[[Category: Horst R]]
[[Category: Ignatov O]]
[[Category: Nishiyama M]]
[[Category: Vetsch M]]
[[Category: Wuthrich K]]