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1o9z

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[[Image:1o9z.jpg|left|200px]]<br /><applet load="1o9z" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1o9z.jpg|left|200px]]
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caption="1o9z, resolution 1.75&Aring;" />
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'''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI (LIGAND FREE)'''<br />
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{{Structure
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|PDB= 1o9z |SIZE=350|CAPTION= <scene name='initialview01'>1o9z</scene>, resolution 1.75&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI (LIGAND FREE)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1O9Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1O9Z OCA].
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1O9Z is a [[Single protein]] structure of 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=1O9Z OCA].
==Reference==
==Reference==
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The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine., Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H, Mol Microbiol. 2003 Aug;49(3):705-15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12864853 12864853]
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The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine., Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H, Mol Microbiol. 2003 Aug;49(3):705-15. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12864853 12864853]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: pathogenesis]]
[[Category: pathogenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:07:54 2008''

Revision as of 11:07, 20 March 2008


PDB ID 1o9z

Drag the structure with the mouse to rotate
, resolution 1.75Å
Coordinates: save as pdb, mmCIF, xml



F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI (LIGAND FREE)


Overview

The F17-G adhesin at the tip of flexible F17 fimbriae of enterotoxigenic Escherichia coli mediates binding to N-acetyl-beta-D-glucosamine-presenting receptors on the microvilli of the intestinal epithelium of ruminants. We report the 1.7 A resolution crystal structure of the lectin domain of F17-G, both free and in complex with N-acetylglucosamine. The monosaccharide is bound on the side of the ellipsoid-shaped protein in a conserved site around which all natural variations of F17-G are clustered. A model is proposed for the interaction between F17-fimbriated E. coli and microvilli with enhanced affinity compared with the binding constant we determined for F17-G binding to N-acetylglucosamine (0.85 mM-1). Unexpectedly, the F17-G structure reveals that the lectin domains of the F17-G, PapGII and FimH fimbrial adhesins all share the immunoglobulin-like fold of the structural components (pilins) of their fimbriae, despite lack of any sequence identity. Fold comparisons with pilin and chaperone structures of the chaperone/usher pathway highlight the central role of the C-terminal beta-strand G of the immunoglobulin-like fold and provides new insights into pilus assembly, function and adhesion.

About this Structure

1O9Z is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

The fimbrial adhesin F17-G of enterotoxigenic Escherichia coli has an immunoglobulin-like lectin domain that binds N-acetylglucosamine., Buts L, Bouckaert J, De Genst E, Loris R, Oscarson S, Lahmann M, Messens J, Brosens E, Wyns L, De Greve H, Mol Microbiol. 2003 Aug;49(3):705-15. PMID:12864853

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