1o9z

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o9z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9z OCA], [http://www.ebi.ac.uk/pdbsum/1o9z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o9z RCSB]</span>
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[[Category: pathogenesis]]
[[Category: pathogenesis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:05 2008''

Revision as of 19:42, 30 March 2008


PDB ID 1o9z

Drag the structure with the mouse to rotate
, resolution 1.75Å
Resources: FirstGlance, OCA, PDBsum, RCSB
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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