1kiu

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(New page: 200px<br /><applet load="1kiu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1kiu, resolution 3.0&Aring;" /> '''FimH adhesin Q133N mu...)
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[[Image:1kiu.gif|left|200px]]<br /><applet load="1kiu" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1kiu, resolution 3.0&Aring;" />
 
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'''FimH adhesin Q133N mutant-FimC chaperone complex with methyl-alpha-D-mannose'''<br />
 
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==Overview==
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==FimH adhesin Q133N mutant-FimC chaperone complex with methyl-alpha-D-mannose==
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The first step in the colonization of the human urinary tract by, pathogenic Escherichia coli is the mannose-sensitive binding of FimH, the, adhesin present at the tip of type 1 pili, to the bladder epithelium. We, elucidated crystallographically the interactions of FimH with D-mannose., The unique site binding pocket occupied by D-mannose was probed using, site-directed mutagenesis. All but one of the mutants examined had greatly, diminished mannose-binding activity and had also lost the ability to bind, human bladder cells. The binding activity of the mono-saccharide D-mannose, was delineated from this of mannotriose (Man(alpha 1-3)[Man(alpha, 1-6)]Man) by generating mutants that abolished D-mannose binding but, retained mannotriose binding activity. Our structure/function analysis, demonstrated that the binding of the monosaccharide alpha-D-mannose is the, primary bladder cell receptor for uropathogenic E. coli and that this, event requires a highly conserved FimH binding pocket. The residues in the, FimH mannose-binding pocket were sequenced and found to be invariant in, over 200 uropathogenic strains of E. coli. Only enterohaemorrhagic E. coli, (EHEC) possess a sequence variation within the mannose-binding pocket of, FimH, suggesting a naturally occurring mechanism of attenuation in EHEC, bacteria that would prevent them from being targeted to the urinary tract.
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<StructureSection load='1kiu' size='340' side='right'caption='[[1kiu]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1kiu]] is a 16 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=1KIU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KIU FirstGlance]. <br>
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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]] 3&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MMA:O1-METHYL-MANNOSE'>MMA</scene></td></tr>
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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=1kiu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kiu OCA], [https://pdbe.org/1kiu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kiu RCSB], [https://www.ebi.ac.uk/pdbsum/1kiu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kiu ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
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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/ki/1kiu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1kiu ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1KIU is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MMA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KIU OCA].
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*[[Adhesin 3D structures|Adhesin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Structural basis of tropism of Escherichia coli to the bladder during urinary tract infection., Hung CS, Bouckaert J, Hung D, Pinkner J, Widberg C, DeFusco A, Auguste CG, Strouse R, Langermann S, Waksman G, Hultgren SJ, Mol Microbiol. 2002 May;44(4):903-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12010488 12010488]
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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: Bouckaert, J.]]
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[[Category: Bouckaert J]]
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[[Category: Hung, C.S.]]
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[[Category: Hung CS]]
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[[Category: MMA]]
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[[Category: adhesin-chaperone complex]]
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[[Category: mannose-bound]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:16:30 2007''
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Current revision

FimH adhesin Q133N mutant-FimC chaperone complex with methyl-alpha-D-mannose

PDB ID 1kiu

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