3bwu: Difference between revisions

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[[Image:3bwu.jpg|left|200px]]


{{Structure
==Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)==
|PDB= 3bwu |SIZE=350|CAPTION= <scene name='initialview01'>3bwu</scene>, resolution 1.760&Aring;
<StructureSection load='3bwu' size='340' side='right'caption='[[3bwu]], [[Resolution|resolution]] 1.76&Aring;' scene=''>
|SITE= <scene name='pdbsite=AC1:Edo+Binding+Site+For+Residue+D+126'>AC1</scene>, <scene name='pdbsite=AC2:Edo+Binding+Site+For+Residue+C+206'>AC2</scene>, <scene name='pdbsite=AC3:Edo+Binding+Site+For+Residue+C+207'>AC3</scene>, <scene name='pdbsite=AC4:Edo+Binding+Site+For+Residue+C+208'>AC4</scene>, <scene name='pdbsite=AC5:Edo+Binding+Site+For+Residue+F+5'>AC5</scene>, <scene name='pdbsite=AC6:Edo+Binding+Site+For+Residue+C+209'>AC6</scene>, <scene name='pdbsite=AC7:Edo+Binding+Site+For+Residue+C+210'>AC7</scene>, <scene name='pdbsite=AC8:Edo+Binding+Site+For+Residue+C+211'>AC8</scene>, <scene name='pdbsite=AC9:Edo+Binding+Site+For+Residue+F+9'>AC9</scene>, <scene name='pdbsite=BC1:Edo+Binding+Site+For+Residue+C+212'>BC1</scene>, <scene name='pdbsite=BC2:Edo+Binding+Site+For+Residue+D+127'>BC2</scene>, <scene name='pdbsite=BC3:Edo+Binding+Site+For+Residue+C+213'>BC3</scene>, <scene name='pdbsite=BC4:Edo+Binding+Site+For+Residue+F+155'>BC4</scene> and <scene name='pdbsite=BC5:Peg+Binding+Site+For+Residue+C+214'>BC5</scene>
== Structural highlights ==
|LIGAND= <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene>
<table><tr><td colspan='2'>[[3bwu]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BWU FirstGlance]. <br>
|ACTIVITY=
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.76&#8491;</td></tr>
|GENE= fimC ([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]), fimF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])
<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>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
|DOMAIN=
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3bwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwu OCA], [https://pdbe.org/3bwu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bwu RCSB], [https://www.ebi.ac.uk/pdbsum/3bwu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bwu ProSAT]</span></td></tr>
|RELATEDENTRY=[[1ze3|1ZE3]]
</table>
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3bwu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bwu OCA], [http://www.ebi.ac.uk/pdbsum/3bwu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=3bwu RCSB]</span>
== Function ==
}}
[https://www.uniprot.org/uniprot/FIMC_ECOLI FIMC_ECOLI] Required for the biogenesis of type 1 fimbriae. Binds and interact with FimH.
 
== Evolutionary Conservation ==
'''Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)'''
[[Image:Consurf_key_small.gif|200px|right]]
 
Check<jmol>
 
  <jmolCheckbox>
==Overview==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bw/3bwu_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3bwu ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very similarly, predominantly through hydrophobic interactions. The conserved binding mode at a "hot spot" on the chaperone surface could guide the design of pilus assembly inhibitors.
Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very similarly, predominantly through hydrophobic interactions. The conserved binding mode at a "hot spot" on the chaperone surface could guide the design of pilus assembly inhibitors.


==About this Structure==
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD.,Eidam O, Dworkowski FS, Glockshuber R, Grutter MG, Capitani G FEBS Lett. 2008 Mar 5;582(5):651-5. Epub 2008 Jan 31. PMID:18242189<ref>PMID:18242189</ref>
3BWU 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=3BWU OCA].
 
==Reference==
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD., Eidam O, Dworkowski FS, Glockshuber R, Grutter MG, Capitani G, FEBS Lett. 2008 Mar 5;582(5):651-5. Epub 2008 Jan 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18242189 18242189]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Capitani, G.]]
[[Category: Eidam, O.]]
[[Category: Grutter, M G.]]
[[Category: chaperone]]
[[Category: mebrane protein]]
[[Category: membrane protein]]
[[Category: n-terminal domain]]
[[Category: structural]]
[[Category: structural protein]]
[[Category: ternary complex with chaperone and pilus subunit]]
[[Category: usher]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 05:29:25 2008''
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3bwu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Capitani G]]
[[Category: Eidam O]]
[[Category: Grutter MG]]

Latest revision as of 01:39, 21 November 2024

Crystal structure of the ternary complex of FimD (N-Terminal Domain, FimDN) with FimC and the N-terminally truncated pilus subunit FimF (FimFt)

3bwu, resolution 1.76Å

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