4AUJ: Fimh Lectin Domain Co-crystal With A Alpha-d-mannoside O- Linked To Para Hydroxypropargyl Phenyl

Citation:
Abstract
Antagonists of the FimH adhesin, a protein almost universally present at the extremity of type-1 fimbriae expressed by Escherichia coli, have been abundantly in the spotlight as alternative treatments of urinary tract infections. The antagonists function as bacterial antiadhesives through highly specific alpha-d-mannose binding in a charged and polar pocket at the tip of the FimH lectin domain and by the stacking of alkyl or aromatic moieties substituted on the mannose with two tyrosine residues (Tyr48 and Tyr137) at the entrance of the mannose-binding pocket. Using high-resolution crystal data, interaction energies are calculated for the different observed aromatic stacking modes between the tyrosines and the antagonist. The dispersion component of the interaction energy correlates with the observed electron density. The quantum chemical reactivity descriptors local hardness and polarizability were successfully validated as prediction tools for ligand affinity in the tyrosine gate of FimH and therefore have potential for rapid drug screening.
PDB ID: 4AUJDownload
MMDB ID: 110467
PDB Deposition Date: 2012/5/17
Updated in MMDB: 2013/12
Experimental Method:
x-ray diffraction
Resolution: 1.53  Å
Source Organism:
Similar Structures:
Biological Unit for 4AUJ: monomeric; determined by author and by software (PISA)
Molecular Components in 4AUJ
Label Count Molecule
Protein (1 molecule)
1
Fimh
Molecule annotation
Chemical (1 molecule)
1
1
* Click molecule labels to explore molecular sequence information.

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