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| ==E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me== | | ==E. coli F17a-G lectin domain complex with GlcNAc(beta1-O)Me== |
| <StructureSection load='1zpl' size='340' side='right' caption='[[1zpl]], [[Resolution|resolution]] 1.70Å' scene=''> | | <StructureSection load='1zpl' size='340' side='right'caption='[[1zpl]]' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[1zpl]] is a 2 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=1ZPL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ZPL FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZPL FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAG:BETA-METHYL-N-ACETYL-D-GLUCOSAMINE'>MAG</scene></td></tr> | | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1zpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpl OCA], [https://pdbe.org/1zpl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zpl RCSB], [https://www.ebi.ac.uk/pdbsum/1zpl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpl ProSAT]</span></td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1o9v|1o9v]]</td></tr>
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| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F17G AF022140 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</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=1zpl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zpl OCA], [http://pdbe.org/1zpl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zpl RCSB], [http://www.ebi.ac.uk/pdbsum/1zpl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zpl ProSAT]</span></td></tr> | |
| </table> | | </table> |
| == 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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| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Since the introduction of structural genomics, the protein has been recognized as the most important variable in crystallization. Recent strategies to modify a protein to improve crystal quality have included rationally engineered point mutations, truncations, deletions and fusions. Five naturally occurring variants, differing in 1-18 amino acids, of the 177-residue lectin domain of the F17G fimbrial adhesin were expressed and purified in identical ways. For four out of the five variants crystals were obtained, mostly in non-isomorphous space groups, with diffraction limits ranging between 2.4 and 1.1 A resolution. A comparative analysis of the crystal-packing contacts revealed that the variable amino acids are often involved in lattice contacts and a single amino-acid substitution can suffice to radically change crystal packing. A statistical approach proved reliable to estimate the compatibilities of the variant sequences with the observed crystal forms. In conclusion, natural variation, universally present within prokaryotic species, is a valuable genetic resource that can be favourably employed to enhance the crystallization success rate with considerably less effort than other strategies.
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| Impact of natural variation in bacterial F17G adhesins on crystallization behaviour.,Buts L, Wellens A, Van Molle I, Wyns L, Loris R, Lahmann M, Oscarson S, De Greve H, Bouckaert J Acta Crystallogr D Biol Crystallogr. 2005 Aug;61(Pt 8):1149-59. Epub 2005, Jul 20. PMID:16041081<ref>PMID:16041081</ref>
| | ==See Also== |
| | | *[[Adhesin 3D structures|Adhesin 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 1zpl" style="background-color:#fffaf0;"></div>
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| == References == | |
| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Bacillus coli migula 1895]] | | [[Category: Large Structures]] |
| [[Category: Bouckaert, J]] | | [[Category: Bouckaert J]] |
| [[Category: Buts, L]] | | [[Category: Buts L]] |
| [[Category: Greve, H De]] | | [[Category: De Greve H]] |
| [[Category: Lahmann, M]] | | [[Category: Lahmann M]] |
| [[Category: Loris, R]] | | [[Category: Loris R]] |
| [[Category: Molle, I Van]] | | [[Category: Oscarson S]] |
| [[Category: Oscarson, S]] | | [[Category: Van Molle I]] |
| [[Category: Wellens, A]] | | [[Category: Wellens A]] |
| [[Category: Wyns, L]] | | [[Category: Wyns L]] |
| [[Category: Bacterial adhesion]]
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| [[Category: Cell adhesion]]
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| [[Category: Fimbriae]]
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| [[Category: Lectin]]
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| [[Category: Protein-sugar complex]]
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