2ixq
From Proteopedia
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|GENE= | |GENE= | ||
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+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ixq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ixq OCA], [http://www.ebi.ac.uk/pdbsum/2ixq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ixq RCSB]</span> | ||
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[[Category: upec]] | [[Category: upec]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:50:07 2008'' |
Revision as of 00:50, 31 March 2008
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Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
THE SOLUTION STRUCTURE OF THE INVASIVE TIP COMPLEX FROM AFA-DR FIBRILS
Overview
Afa/Dr family of adhesins are produced by pathogenic Escherichia coli strains that are especially prevalent in chronic diarrhoeal and recurrent urinary tract infections. Most notably, they are found in up to 50% of cystitis cases in children and 30% of pyelonephritis in pregnant women. Afa/Dr adhesins are capped surface fibrils that mediate recognition of the host and subsequent bacterial internalization. Using the newly solved three-dimensional structure of the minimal invasive complex (AfaDE) combined with biochemical and cellular assays, we reveal the architecture of the fibrillar cap and identify a novel mode of synergistic integrin recognition.
About this Structure
2IXQ is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
The solution structure of the invasive tip complex from Afa/Dr fibrils., Cota E, Jones C, Simpson P, Altroff H, Anderson KL, du Merle L, Guignot J, Servin A, Le Bouguenec C, Mardon H, Matthews S, Mol Microbiol. 2006 Oct;62(2):356-66. Epub 2006 Sep 8. PMID:16965519
Page seeded by OCA on Mon Mar 31 03:50:07 2008
Categories: Protein complex | Altroff, H. | Anderson, K L. | Bouguenec, C Le. | Cota, E. | Guignot, J. | Jones, C. | Mardon, H. | Matthews, S. | Merle, L Du. | Servin, A. | Simpson, P. | Afae | Afimbrial sheath | Cell adhesion | Daec | Daf | Donor strand complemented | Fimbria | Ig-like domain | Structural protein | Upec