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- | [[Image:1o9v.gif|left|200px]] | + | {{Seed}} |
| + | [[Image:1o9v.png|left|200px]] |
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| {{STRUCTURE_1o9v| PDB=1o9v | SCENE= }} | | {{STRUCTURE_1o9v| PDB=1o9v | SCENE= }} |
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- | '''F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE'''
| + | ===F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE=== |
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- | ==Overview==
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- | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12864853}}, adds the Publication Abstract to the page |
| + | (as it appears on PubMed at http://www.pubmed.gov), where 12864853 is the PubMed ID number. |
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| + | {{ABSTRACT_PUBMED_12864853}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Lectin]] | | [[Category: Lectin]] |
| [[Category: Pathogenesis]] | | [[Category: Pathogenesis]] |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:34:08 2008'' | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:13:18 2008'' |
Revision as of 07:13, 28 July 2008
Template:STRUCTURE 1o9v
F17-AG LECTIN DOMAIN FROM ESCHERICHIA COLI IN COMPLEX WITH A SELENIUM CARBOHYDRATE DERIVATIVE
Template:ABSTRACT PUBMED 12864853
About this Structure
1O9V 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
Page seeded by OCA on Mon Jul 28 10:13:18 2008
Categories: Escherichia coli | Single protein | Bouckaert, J. | Brosens, E. | Buts, L. | Genst, E De. | Greve, H De. | Lahmann, M. | Loris, R. | Messens, J. | Oscarson, S. | Wyns, L. | Bacterial adhesin | Bacterial attachment | Immunoglobulin fold | Lectin | Pathogenesis