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4avi

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Revision as of 07:22, 11 August 2016

Structure of the FimH lectin domain in the trigonal space group, in complex with a methyl ester octyl alpha-D-mannoside at 2.4 A resolution

Structural highlights

4avi is a 2 chain structure with sequence from Ecout. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	4att, 4auj, 4auu, 4auy, 4av0, 4av4, 4av5, 4avh, 4avj, 4avk
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Publication Abstract from PubMed

Uropathogenic Escherichia coli (UPEC) are the major causative agents of urinary tract infections. During infection, UPEC adhere to mannosylated glycoreceptors on the urothelium via the FimH adhesin located at the tip of type 1 pili. Synthetic FimH antiadhesives such as alkyl and phenyl alpha-d-mannopyranosides are thus ideal candidates for the chemical interception of this crucial step in pathogenesis. The crystal structures of the FimH lectin domain in its ligand-free form and in complexes with eight medium- and high-affinity mannopyranoside inhibitors are presented. The thermodynamic profiles of the FimH-inhibitor interactions indicate that the binding of FimH to alpha-d-mannopyranose is enthalpy-driven and has a negative entropic change. Addition of a hydrophobic aglycon influences the binding enthalpy and can induce a favorable entropic change. The alleviation of the entropic cost is at least in part explained by increased dynamics in the tyrosine gate (Tyr48 and Tyr137) of the FimH receptor-binding site upon binding of the ligand. Ligands with a phenyl group directly linked to the anomeric oxygen of alpha-d-mannose introduce the largest dynamics into the Tyr48 side chain, because conjugation with the anomeric oxygen of alpha-d-mannose forces the aromatic aglycon into a conformation that comes into close contact ( approximately 2.65 A) with Tyr48. A propargyl group in this position predetermines the orientation of the aglycon and significantly decreases affinity. FimH has the highest affinity for alpha-d-mannopyranosides substituted with hydrophobic aglycons that are compatible in shape and electrostatic properties to the tyrosine gate, such as heptyl alpha-d-mannose.

The Tyrosine Gate as a Potential Entropic Lever in the Receptor-Binding Site of the Bacterial Adhesin FimH.,Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J Biochemistry. 2012 Jun 7. PMID:22657089^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Wellens A, Lahmann M, Touaibia M, Vaucher J, Oscarson S, Roy R, Remaut H, Bouckaert J. The Tyrosine Gate as a Potential Entropic Lever in the Receptor-Binding Site of the Bacterial Adhesin FimH. Biochemistry. 2012 Jun 7. PMID:22657089 doi:10.1021/bi300251r

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4avi"

@@ Line 1: / Line 1: @@
 ==Structure of the FimH lectin domain in the trigonal space group, in complex with a methyl ester octyl alpha-D-mannoside at 2.4 A resolution==
 <StructureSection load='4avi' size='340' side='right' caption='[[4avi]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4avi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4avi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecout Ecout]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AVI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AVI FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=XNS:METHYL+ESTER+OCTYL+ALPHA-1O-D-MANNOPYRANNOSIDE'>XNS</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4att|4att]], [[4auj|4auj]], [[4auu|4auu]], [[4auy|4auy]], [[4av0|4av0]], [[4av4|4av4]], [[4av5|4av5]], [[4avh|4avh]], [[4avj|4avj]], [[4avk|4avk]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4avi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4avi RCSB], [http://www.ebi.ac.uk/pdbsum/4avi PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4avi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avi OCA], [http://pdbe.org/4avi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4avi RCSB], [http://www.ebi.ac.uk/pdbsum/4avi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4avi ProSAT]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 15: / Line 16: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 4avi" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Escherichia coli]]
+[[Category: Ecout]]
 [[Category: Bouckaert, J]]
 [[Category: Lahmann, M]]

4avi

From Proteopedia

Revision as of 07:22, 11 August 2016

Structure of the FimH lectin domain in the trigonal space group, in complex with a methyl ester octyl alpha-D-mannoside at 2.4 A resolution

Structural highlights

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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