1o9v
From Proteopedia
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| - | [[Image:1o9v.gif|left|200px]]<br /> | + | [[Image:1o9v.gif|left|200px]]<br /><applet load="1o9v" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1o9v" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1o9v, resolution 1.75Å" /> | caption="1o9v, resolution 1.75Å" /> | ||
'''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE'''<br /> | '''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1O9V 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 SNG as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1O9V 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 SNG as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Site: <scene name='pdbsite=AC1:Sng Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1O9V OCA]. |
==Reference== | ==Reference== | ||
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[[Category: pathogenesis]] | [[Category: pathogenesis]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 17:11:49 2007'' |
Revision as of 15:02, 18 December 2007
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F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE
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
1O9V is a Single protein structure of sequence from Escherichia coli with SNG as ligand. Known structural/functional Site: . 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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