1o9z
From Proteopedia
(New page: 200px<br /><applet load="1o9z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o9z, resolution 1.75Å" /> '''F17-AG LECTIN DOMAIN...) |
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| - | [[Image:1o9z.jpg|left|200px]]<br /><applet load="1o9z" size=" | + | [[Image:1o9z.jpg|left|200px]]<br /><applet load="1o9z" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1o9z, resolution 1.75Å" /> | caption="1o9z, resolution 1.75Å" /> | ||
'''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI (LIGAND FREE)'''<br /> | '''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI (LIGAND FREE)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The F17-G adhesin at the tip of flexible F17 fimbriae of enterotoxigenic | + | 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== | ==About this Structure== | ||
| - | 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: Brosens, E.]] | [[Category: Brosens, E.]] | ||
[[Category: Buts, L.]] | [[Category: Buts, L.]] | ||
| - | [[Category: Genst, E | + | [[Category: Genst, E De.]] |
| - | [[Category: Greve, H | + | [[Category: Greve, H De.]] |
[[Category: Lahmann, M.]] | [[Category: Lahmann, M.]] | ||
[[Category: Loris, R.]] | [[Category: Loris, R.]] | ||
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[[Category: pathogenesis]] | [[Category: pathogenesis]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:15:11 2008'' |
Revision as of 12:15, 21 February 2008
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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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