1o9v
From Proteopedia
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|PDB= 1o9v |SIZE=350|CAPTION= <scene name='initialview01'>1o9v</scene>, resolution 1.75Å | |PDB= 1o9v |SIZE=350|CAPTION= <scene name='initialview01'>1o9v</scene>, resolution 1.75Å | ||
|SITE= <scene name='pdbsite=AC1:Sng+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Sng+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SNG:METHYL 2-ACETAMIDO-1,2-DIDEOXY-1-SELENO-BETA-D-GLUCOPYRANOSIDE'>SNG</scene> | + | |LIGAND= <scene name='pdbligand=SNG:METHYL+2-ACETAMIDO-1,2-DIDEOXY-1-SELENO-BETA-D-GLUCOPYRANOSIDE'>SNG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1o9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1o9v OCA], [http://www.ebi.ac.uk/pdbsum/1o9v PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1o9v RCSB]</span> | ||
}} | }} | ||
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[[Category: Oscarson, S.]] | [[Category: Oscarson, S.]] | ||
[[Category: Wyns, L.]] | [[Category: Wyns, L.]] | ||
| - | [[Category: SNG]] | ||
[[Category: bacterial adhesin]] | [[Category: bacterial adhesin]] | ||
[[Category: bacterial attachment]] | [[Category: bacterial attachment]] | ||
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[[Category: pathogenesis]] | [[Category: pathogenesis]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:42:02 2008'' |
Revision as of 19:42, 30 March 2008
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| , resolution 1.75Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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