View source for 4z3e


==Crystal structure of the lectin domain of PapG from E. coli BI47 in complex with SSEA4 in space group P212121==
<StructureSection load='4z3e' size='340' side='right'caption='[[4z3e]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4z3e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Z3E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Z3E 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]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=GLA:ALPHA+D-GALACTOSE'>GLA</scene>, <scene name='pdbligand=NGA:N-ACETYL-D-GALACTOSAMINE'>NGA</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=4z3e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4z3e OCA], [https://pdbe.org/4z3e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4z3e RCSB], [https://www.ebi.ac.uk/pdbsum/4z3e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4z3e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A182DW20_ECOLX A0A182DW20_ECOLX] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Uropathogenic E. coli exploit the PapG-II adhesin for infecting host cells of the kidney; moreover, the expression of PapG-II located at the tip of bacterial pili has been correlated with the onset of pyelonephritis in humans, a potentially life-threatening condition. It was envisaged that the blocking of PapG-II, and thus bacterial adhesion, embodies a viable therapeutic alternative to conventional antibiotic treatment. Within our search for potent PapG-II antagonists, we observed an increase in affinity when tetrasaccharide 1, the natural ligand of PapG-II in human kidneys, was elongated to hexasaccharide 2, although the additional Siaalpha(2-3)Gal extension is not in direct contact with the lectin. ITC studies suggest that the increased affinity results from partial desolvation of non-binding regions of the hexasaccharide, and is ultimately connected to the perturbation of outer hydration layers. Our results are in agreement with previous observations and suggest a general mechanism for modulating carbohydrate-protein interactions based on non-binding regions of the ligand.

Carbohydrate-Lectin Interactions - An Unexpected Contribution to Affinity.,Navarra G, Zihlmann P, Jakob RP, Stangier K, Preston RC, Rabbani S, Smiesko M, Wagner B, Maier T, Ernst B Chembiochem. 2017 Jan 11. doi: 10.1002/cbic.201600615. PMID:28076665<ref>PMID:28076665</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4z3e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Ernst B]]
[[Category: Jakob RP]]
[[Category: Maier T]]
[[Category: Navarra G]]
[[Category: Preston RC]]
[[Category: Rabbani S]]
[[Category: Stangier K]]
[[Category: Zihlmann P]]