3zpd: Difference between revisions
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==Solution structure of the FimH adhesin carbohydrate-binding domain== | |||
<StructureSection load='3zpd' size='340' side='right'caption='[[3zpd]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3zpd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_J96 Escherichia coli J96]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZPD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZPD FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 25 models</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=3zpd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zpd OCA], [https://pdbe.org/3zpd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zpd RCSB], [https://www.ebi.ac.uk/pdbsum/3zpd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zpd ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A2IC68_ECOLX A2IC68_ECOLX] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Uropathogenic Escherichia coli cause urinary tract infections by adhering to mannosylated receptors on the human urothelium via the carbohydrate-binding domain of the FimH adhesin (FimHL). Numerous alpha-d-mannopyranosides, including alpha-d-heptyl mannose (HM), inhibit this process by interacting with FimHL. To establish the molecular basis of the high-affinity HM binding, we solved the solution structure of the apo form and the crystal structure of the FimHL-HM complex. NMR relaxation analysis revealed that protein dynamics were not affected by the sugar binding, yet HM addition promoted protein dimerization, which was further confirmed by small-angle X-ray scattering. Finally, to address the role of Y48, part of the "tyrosine gate" believed to govern the affinity and specificity of mannoside binding, we characterized the FimHL Y48A mutant, whose conformational, dynamical, and HM binding properties were found to be very similar to those of the wild-type protein. | |||
Study of the Structural and Dynamic Effects in the FimH Adhesin upon alpha-d-Heptyl Mannose Binding.,Vanwetswinkel S, Volkov AN, Sterckx YG, Garcia-Pino A, Buts L, Vranken WF, Bouckaert J, Roy R, Wyns L, van Nuland NA J Med Chem. 2014 Feb 7. PMID:24476493<ref>PMID:24476493</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3zpd" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli J96]] | |||
[[Category: Large Structures]] | |||
[[Category: Buts L]] | |||
[[Category: Vanwetswinkel S]] | |||
[[Category: Vranken WF]] | |||
[[Category: Van Nuland NAJ]] | |||
Latest revision as of 05:39, 21 November 2024
Solution structure of the FimH adhesin carbohydrate-binding domainSolution structure of the FimH adhesin carbohydrate-binding domain
Structural highlights
FunctionPublication Abstract from PubMedUropathogenic Escherichia coli cause urinary tract infections by adhering to mannosylated receptors on the human urothelium via the carbohydrate-binding domain of the FimH adhesin (FimHL). Numerous alpha-d-mannopyranosides, including alpha-d-heptyl mannose (HM), inhibit this process by interacting with FimHL. To establish the molecular basis of the high-affinity HM binding, we solved the solution structure of the apo form and the crystal structure of the FimHL-HM complex. NMR relaxation analysis revealed that protein dynamics were not affected by the sugar binding, yet HM addition promoted protein dimerization, which was further confirmed by small-angle X-ray scattering. Finally, to address the role of Y48, part of the "tyrosine gate" believed to govern the affinity and specificity of mannoside binding, we characterized the FimHL Y48A mutant, whose conformational, dynamical, and HM binding properties were found to be very similar to those of the wild-type protein. Study of the Structural and Dynamic Effects in the FimH Adhesin upon alpha-d-Heptyl Mannose Binding.,Vanwetswinkel S, Volkov AN, Sterckx YG, Garcia-Pino A, Buts L, Vranken WF, Bouckaert J, Roy R, Wyns L, van Nuland NA J Med Chem. 2014 Feb 7. PMID:24476493[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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