1qun

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(New page: 200px<br /><applet load="1qun" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qun, resolution 2.8&Aring;" /> '''X-RAY STRUCTURE OF TH...)
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[[Image:1qun.gif|left|200px]]<br /><applet load="1qun" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qun, resolution 2.8&Aring;" />
 
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'''X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI'''<br />
 
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==Overview==
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==X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI==
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Type 1 pili-adhesive fibers expressed in most members of the, Enterobacteriaceae family-mediate binding to mannose receptors on host, cells through the FimH adhesin. Pilus biogenesis proceeds by way of the, chaperone/usher pathway. The x-ray structure of the FimC-FimH, chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5, angstrom resolution reveals the basis for carbohydrate recognition and for, pilus assembly. The carboxyl-terminal pilin domain of FimH has an, immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand, complementation mechanism in which the chaperone donates a strand to, complete the pilin domain explains the basis for both chaperone function, and pilus biogenesis.
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<StructureSection load='1qun' size='340' side='right'caption='[[1qun]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qun]] 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=1QUN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QUN 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]] 2.8&#8491;</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=1qun FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qun OCA], [https://pdbe.org/1qun PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qun RCSB], [https://www.ebi.ac.uk/pdbsum/1qun PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qun 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/qu/1qun_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=1qun 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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Type 1 pili-adhesive fibers expressed in most members of the Enterobacteriaceae family-mediate binding to mannose receptors on host cells through the FimH adhesin. Pilus biogenesis proceeds by way of the chaperone/usher pathway. The x-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli at 2.5 angstrom resolution reveals the basis for carbohydrate recognition and for pilus assembly. The carboxyl-terminal pilin domain of FimH has an immunoglobulin-like fold, except that the seventh strand is missing, leaving part of the hydrophobic core exposed. A donor strand complementation mechanism in which the chaperone donates a strand to complete the pilin domain explains the basis for both chaperone function and pilus biogenesis.
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==About this Structure==
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X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli.,Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, Hultgren SJ, Knight SD Science. 1999 Aug 13;285(5430):1061-6. PMID:10446051<ref>PMID:10446051</ref>
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1QUN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QUN OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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X-ray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli., Choudhury D, Thompson A, Stojanoff V, Langermann S, Pinkner J, Hultgren SJ, Knight SD, Science. 1999 Aug 13;285(5430):1061-6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10446051 10446051]
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</div>
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[[Category: Escherichia coli]]
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<div class="pdbe-citations 1qun" style="background-color:#fffaf0;"></div>
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[[Category: Protein complex]]
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[[Category: Choudhury, D.]]
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[[Category: Hultgren, S.J.]]
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[[Category: Knight, S.]]
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[[Category: Langerman, S.]]
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[[Category: Pinkner, J.]]
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[[Category: Stojanoff, V.]]
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[[Category: Thompson, A.]]
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[[Category: chaperone adhesin donor strand complementation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:00:17 2007''
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==See Also==
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*[[Adhesin 3D structures|Adhesin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Escherichia coli]]
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[[Category: Large Structures]]
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[[Category: Choudhury D]]
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[[Category: Hultgren SJ]]
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[[Category: Knight S]]
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[[Category: Langerman S]]
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[[Category: Pinkner J]]
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[[Category: Stojanoff V]]
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[[Category: Thompson A]]

Current revision

X-RAY STRUCTURE OF THE FIMC-FIMH CHAPERONE ADHESIN COMPLEX FROM UROPATHOGENIC E.COLI

PDB ID 1qun

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