1klf: Difference between revisions

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[[Image:1klf.gif|left|200px]]
{{Seed}}
[[Image:1klf.png|left|200px]]


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{{STRUCTURE_1klf|  PDB=1klf  |  SCENE=  }}  
{{STRUCTURE_1klf|  PDB=1klf  |  SCENE=  }}  


'''FIMH ADHESIN-FIMC CHAPERONE COMPLEX WITH D-MANNOSE'''
===FIMH ADHESIN-FIMC CHAPERONE COMPLEX WITH D-MANNOSE===




==Overview==
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The first step in the colonization of the human urinary tract by pathogenic Escherichia coli is the mannose-sensitive binding of FimH, the adhesin present at the tip of type 1 pili, to the bladder epithelium. We elucidated crystallographically the interactions of FimH with D-mannose. The unique site binding pocket occupied by D-mannose was probed using site-directed mutagenesis. All but one of the mutants examined had greatly diminished mannose-binding activity and had also lost the ability to bind human bladder cells. The binding activity of the mono-saccharide D-mannose was delineated from this of mannotriose (Man(alpha 1-3)[Man(alpha 1-6)]Man) by generating mutants that abolished D-mannose binding but retained mannotriose binding activity. Our structure/function analysis demonstrated that the binding of the monosaccharide alpha-D-mannose is the primary bladder cell receptor for uropathogenic E. coli and that this event requires a highly conserved FimH binding pocket. The residues in the FimH mannose-binding pocket were sequenced and found to be invariant in over 200 uropathogenic strains of E. coli. Only enterohaemorrhagic E. coli (EHEC) possess a sequence variation within the mannose-binding pocket of FimH, suggesting a naturally occurring mechanism of attenuation in EHEC bacteria that would prevent them from being targeted to the urinary tract.
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{{ABSTRACT_PUBMED_12010488}}


==About this Structure==
==About this Structure==
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[[Category: Adhesin-chaperone complex]]
[[Category: Adhesin-chaperone complex]]
[[Category: Mannose-bound]]
[[Category: Mannose-bound]]
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