1oio
From Proteopedia
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| - | [[ | + | ==GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI== |
| + | <StructureSection load='1oio' size='340' side='right' caption='[[1oio]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1oio]] is a 2 chain structure with sequence 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=1OIO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OIO FirstGlance]. <br> | ||
| + | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br> | ||
| + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1oio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oio OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1oio RCSB], [http://www.ebi.ac.uk/pdbsum/1oio PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | GafD in Escherichia coli G (F17) fimbriae is associated with diarrheal disease, and the structure of the ligand-binding domain, GafD1-178, has been determined at 1.7A resolution in the presence of the receptor sugar N-acetyl-D-glucosamine. The overall fold is a beta-barrel jelly-roll fold. The ligand-binding site was identified and localized to the side of the molecule. Receptor binding is mediated by side-chain as well main-chain interactions. Ala43-Asn44, Ser116-Thr117 form the sugar acetamide specificity pocket, while Asp88 confers tight binding and Trp109 appears to position the ligand. There is a disulfide bond that rigidifies the acetamide specificity pocket. The three fimbrial lectins, GafD, FimH and PapG share similar beta-barrel folds but display different ligand-binding regions and disulfide-bond patterns. We suggest an evolutionary path for the evolution of the very diverse fimbrial lectins from a common ancestral fold. | ||
| - | + | The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia.,Merckel MC, Tanskanen J, Edelman S, Westerlund-Wikstrom B, Korhonen TK, Goldman A J Mol Biol. 2003 Aug 22;331(4):897-905. PMID:12909017<ref>PMID:12909017</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | == | + | __TOC__ |
| - | + | </StructureSection> | |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Edelman, S.]] | [[Category: Edelman, S.]] | ||
Revision as of 15:05, 28 September 2014
GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI
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