View source for 4buq


==Crystal structure of wild type FimH lectin domain in complex with heptyl alpha-D-mannopyrannoside==
<StructureSection load='4buq' size='340' side='right'caption='[[4buq]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4buq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_UTI89 Escherichia coli UTI89]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.199&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KGM:HEPTYL+ALPHA-D-MANNOPYRANNOSIDE'>KGM</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4buq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buq OCA], [https://pdbe.org/4buq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4buq RCSB], [https://www.ebi.ac.uk/pdbsum/4buq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4buq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A2IC68_ECOLX A2IC68_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.

Validation of Reactivity Descriptors to Assess the Aromatic Stacking within the Tyrosine Gate of FimH.,Roos G, Wellens A, Touaibia M, Yamakawa N, Geerlings P, Roy R, Wyns L, Bouckaert J ACS Med Chem Lett. 2013 Sep 13;4(11):1085-90. doi: 10.1021/ml400269v. eCollection, 2013 Nov 14. PMID:24900609<ref>PMID:24900609</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4buq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli UTI89]]
[[Category: Large Structures]]
[[Category: Bouckaert J]]
[[Category: Eid S]]
[[Category: Ernst B]]
[[Category: Glockshuber R]]
[[Category: Preston R]]
[[Category: Puorger C]]
[[Category: Rabbani S]]
[[Category: Thompson A]]
[[Category: Zalewski A]]