3f64

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<StructureSection load='3f64' size='340' side='right'caption='[[3f64]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
<StructureSection load='3f64' size='340' side='right'caption='[[3f64]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3f64]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3F64 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3F64 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3f64]] is a 1 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=3F64 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3F64 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEC:N-[(2S,3R,4R,5S,6R)-4,5-DIHYDROXY-6-(HYDROXYMETHYL)-2-(4-NITROPHENOXY)OXAN-3-YL]ETHANAMIDE'>LEC</scene></td></tr>
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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]] 1.95&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o9z|1o9z]]</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=LEC:N-[(2S,3R,4R,5S,6R)-4,5-DIHYDROXY-6-(HYDROXYMETHYL)-2-(4-NITROPHENOXY)OXAN-3-YL]ETHANAMIDE'>LEC</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3f64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f64 OCA], [http://pdbe.org/3f64 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3f64 RCSB], [http://www.ebi.ac.uk/pdbsum/3f64 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3f64 ProSAT]</span></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=3f64 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3f64 OCA], [https://pdbe.org/3f64 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3f64 RCSB], [https://www.ebi.ac.uk/pdbsum/3f64 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3f64 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/F17AG_ECOLX F17AG_ECOLX]] Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes.
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[https://www.uniprot.org/uniprot/F17AG_ECOLX F17AG_ECOLX] Essential fimbrial adhesion factor that mediates binding to N-acetylglucosamine-containing receptors in the host intestinal microvilli, leading to colonization of the intestinal tissue, and diarrhea or septicemia. Also confers adhesiveness to laminin and basement membranes.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Fimbriae are long, proteinaceous adhesion organelles expressed on the bacterial envelope, evolutionarily adapted by Escherichia coli strains for the colonization of epithelial linings. Using glycan arrays of the Consortium for Functional Glycomics (CFG), the lectin domains were screened of the fimbrial adhesins F17G and FedF from enterotoxigenic E. coli (ETEC) and of the FimH adhesin from uropathogenic E. coli. This has led to the discovery of a more specific receptor for F17G, GlcNAcb1,3Gal. No significant differences emerged from the glycan binding profiles of the F17G lectin domains from five different E. coli strains. However, strain-dependent amino acid variations, predominantly towards the positively charged arginine, were indicated by sulfate binding in FedF and F17G crystal structures. For FedF, no significant binders could be observed on the CFG glycan array. Hence, a shotgun array was generated from microvilli scrapings of the distal jejunum of a 3-week old piglet about to be weaned. On this array, the blood group A type 1 hexasaccharide emerged as a receptor for the FedF lectin domain and remarkably also for F18-fimbriated E. coli. F17G was found to selectively recognize glycan species with a terminal GlcNAc, typifying intestinal mucins. In conclusion, F17G and FedF recognize long glycan sequences that could only be identified using the shotgun approach. Interestingly, ETEC strains display a large capacity to adapt their fimbrial adhesins to ecological niches via charge-driven interactions, congruent with binding to thick mucosal surfaces displaying an acidic gradient along the intestinal tract.
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Structural Sampling of Glycan Interaction Profiles Reveals Mucosal Receptors for Fimbrial Adhesins of Enterotoxigenic Escherichia coli.,Lonardi E, Moonens K, Buts L, de Boer AR, Olsson JD, Weiss MS, Fabre E, Guerardel Y, Deelder AM, Oscarson S, Wuhrer M, Bouckaert J Biology (Basel). 2013 Jul 1;2(3):894-917. doi: 10.3390/biology2030894. PMID:24833052<ref>PMID:24833052</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 3f64" style="background-color:#fffaf0;"></div>
==See Also==
==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
*[[Adhesin 3D structures|Adhesin 3D structures]]
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Boer, A De]]
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[[Category: Bouckaert J]]
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[[Category: Bouckaert, J]]
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[[Category: Buts L]]
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[[Category: Buts, L]]
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[[Category: De Boer A]]
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[[Category: Genst, E De]]
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[[Category: De Genst E]]
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[[Category: Greve, H De]]
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[[Category: De Greve H]]
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[[Category: Guerardel, Y]]
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[[Category: De Kerpel M]]
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[[Category: Jonckheere, W]]
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[[Category: Guerardel Y]]
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[[Category: Kerpel, M De]]
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[[Category: Jonckheere W]]
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[[Category: Olsson, J D.M]]
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[[Category: Olsson JDM]]
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[[Category: Oscarson, S]]
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[[Category: Oscarson S]]
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[[Category: Willaert, R]]
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[[Category: Willaert R]]
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[[Category: Wuhrer, M]]
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[[Category: Wuhrer M]]
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[[Category: Wyns, L]]
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[[Category: Wyns L]]
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[[Category: Bacterial adhesin]]
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[[Category: Bacterial attachment]]
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[[Category: Cell projection]]
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[[Category: Fimbrium]]
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[[Category: Immunoglobulin fold]]
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[[Category: Lectin]]
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[[Category: Pathogenesis]]
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[[Category: Sugar binding protein]]
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Current revision

F17a-G lectin domain with bound GlcNAc(beta1-O)paranitrophenyl ligand

PDB ID 3f64

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