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[[Image:1oio.jpg|left|200px]]<br /><applet load="1oio" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1oio, resolution 1.70&Aring;" />
'''GAFD (F17C-TYPE) FIMBRIAL ADHESIN FROM ESCHERICHIA COLI'''<br />


==Overview==
==GafD (F17c-type) Fimbrial adhesin from Escherichia coli==
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.
<StructureSection load='1oio' size='340' side='right'caption='[[1oio]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oio]] is a 2 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=1OIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OIO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=1oio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oio OCA], [https://pdbe.org/1oio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oio RCSB], [https://www.ebi.ac.uk/pdbsum/1oio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oio ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F17GG_ECOLX F17GG_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. May be involved in the initiation of polymerization of fimbrillin monomers during fimbrial filament biogenesis.<ref>PMID:7883703</ref> <ref>PMID:8698525</ref>
<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.


==About this Structure==
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>
1OIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Nag+Binding+Site+For+Chain+B'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OIO OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12909017 12909017]
</div>
<div class="pdbe-citations 1oio" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Adhesin 3D structures|Adhesin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Edelman, S.]]
[[Category: Edelman S]]
[[Category: Goldman, A.]]
[[Category: Goldman A]]
[[Category: Korhonen, T.K.]]
[[Category: Korhonen TK]]
[[Category: Merckel, M.C.]]
[[Category: Merckel MC]]
[[Category: Tanskanen, J.]]
[[Category: Tanskanen J]]
[[Category: Westerlund-Wikstrom, B.]]
[[Category: Westerlund-Wikstrom B]]
[[Category: NAG]]
[[Category: adhesin]]
[[Category: glcnac binding lectin]]
[[Category: n-acetyl-d-glucosamine binding]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:58:36 2008''

Latest revision as of 11:42, 6 November 2024

GafD (F17c-type) Fimbrial adhesin from Escherichia coliGafD (F17c-type) Fimbrial adhesin from Escherichia coli

Structural highlights

1oio is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.7Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

F17GG_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. May be involved in the initiation of polymerization of fimbrillin monomers during fimbrial filament biogenesis.[1] [2]

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[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Saarela S, Taira S, Nurmiaho-Lassila EL, Makkonen A, Rhen M. The Escherichia coli G-fimbrial lectin protein participates both in fimbrial biogenesis and in recognition of the receptor N-acetyl-D-glucosamine. J Bacteriol. 1995 Mar;177(6):1477-84. PMID:7883703
  2. ↑ Saarela S, Westerlund-Wikstrom B, Rhen M, Korhonen TK. The GafD protein of the G (F17) fimbrial complex confers adhesiveness of Escherichia coli to laminin. Infect Immun. 1996 Jul;64(7):2857-60. PMID:8698525
  3. ↑ Merckel MC, Tanskanen J, Edelman S, Westerlund-Wikstrom B, Korhonen TK, Goldman A. The structural basis of receptor-binding by Escherichia coli associated with diarrhea and septicemia. J Mol Biol. 2003 Aug 22;331(4):897-905. PMID:12909017

1oio, resolution 1.70Å

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