4BUQ
Crystal structure of wild type FimH lectin domain in complex with heptyl alpha-D-mannopyrannoside
Summary for 4BUQ
| Entry DOI | 10.2210/pdb4buq/pdb |
| Descriptor | FIMH, heptyl alpha-D-mannopyranoside (3 entities in total) |
| Functional Keywords | cell adhesion, type 1 fimbriae, urinary tract infection, variable immunoglobulin fold |
| Biological source | ESCHERICHIA COLI UTI89 |
| Total number of polymer chains | 2 |
| Total formula weight | 34390.34 |
| Authors | Rabbani, S.,Bouckaert, J.,Zalewski, A.,Preston, R.,Eid, S.,Thompson, A.,Puorger, C.,Glockshuber, R.,Ernst, B. (deposition date: 2013-06-23, release date: 2014-02-19, Last modification date: 2024-10-16) |
| Primary citation | Roos, G.,Wellens, A.,Touaibia, M.,Yamakawa, N.,Geerlings, P.,Roy, R.,Wyns, L.,Bouckaert, J. Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of Fimh Acs Med.Chem.Lett., 4:1085-, 2013 Cited by PubMed 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 α-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. PubMed: 24900609DOI: 10.1021/ML400269V PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.199 Å) |
Structure validation
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