1ze3

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[[Image:1ze3.gif|left|200px]]
 
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{{Structure
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==Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH==
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|PDB= 1ze3 |SIZE=350|CAPTION= <scene name='initialview01'>1ze3</scene>, resolution 1.84&Aring;
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<StructureSection load='1ze3' size='340' side='right'caption='[[1ze3]], [[Resolution|resolution]] 1.84&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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<table><tr><td colspan='2'>[[1ze3]] is a 3 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=1ZE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZE3 FirstGlance]. <br>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84&#8491;</td></tr>
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|GENE= fimC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimH ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]), fimD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
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}}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ze3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ze3 OCA], [https://pdbe.org/1ze3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ze3 RCSB], [https://www.ebi.ac.uk/pdbsum/1ze3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ze3 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ze/1ze3_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1ze3 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ze3" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Adhesin 3D structures|Adhesin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1ZE3 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZE3 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15920478 15920478]
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[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
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[[Category: Protein complex]]
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[[Category: Large Structures]]
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[[Category: Bettendorff, P.]]
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[[Category: Bettendorff P]]
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[[Category: Capitani, G.]]
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[[Category: Capitani G]]
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[[Category: Eidam, O.]]
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[[Category: Eidam O]]
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[[Category: Glockshuber, R.]]
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[[Category: Glockshuber R]]
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[[Category: Grutter, M G.]]
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[[Category: Grutter MG]]
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[[Category: Herrmann, T.]]
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[[Category: Herrmann T]]
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[[Category: Horst, R.]]
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[[Category: Horst R]]
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[[Category: Ignatov, O.]]
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[[Category: Ignatov O]]
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[[Category: Jelesarov, I.]]
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[[Category: Jelesarov I]]
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[[Category: Nishiyama, M.]]
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[[Category: Nishiyama M]]
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[[Category: Vetsch, M.]]
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[[Category: Vetsch M]]
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[[Category: Wuthrich, K.]]
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[[Category: Wuthrich K]]
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[[Category: EDO]]
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[[Category: soluble domain]]
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[[Category: ternary complex with chaperone and pilus subunit]]
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[[Category: usher]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:22 2008''
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Current revision

Crystal Structure of the Ternary Complex of FIMD (N-Terminal Domain) with FIMC and the Pilin Domain of FIMH

PDB ID 1ze3

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