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4avi

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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 Escherichia coli UTI89. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

FIMH_ECOLI Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.

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 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 3: / Line 3: @@
 <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 [https://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 [https://proteopedia.org/fgij/fg.htm?mol=4AVI FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4avi]] 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=4AVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AVI FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4att|4att]], [[4auj|4auj]], [[4auu|4auu]], [[4auy|4auy]], [[4av0|4av0]], [[4av4|4av4]], [[4av5|4av5]], [[4avh|4avh]], [[4avj|4avj]], [[4avk|4avk]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4avi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4avi OCA], [https://pdbe.org/4avi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4avi RCSB], [https://www.ebi.ac.uk/pdbsum/4avi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4avi ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/FIMH_ECOLI FIMH_ECOLI] Involved in regulation of length and mediation of adhesion of type 1 fimbriae (but not necessary for the production of fimbriae). Adhesin responsible for the binding to D-mannose. It is laterally positioned at intervals in the structure of the type 1 fimbriae. In order to integrate FimH in the fimbriae FimF and FimG are needed.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 26: @@
 __TOC__
 </StructureSection>
-[[Category: Ecout]]
+[[Category: Escherichia coli UTI89]]
 [[Category: Large Structures]]
-[[Category: Bouckaert, J]]
+[[Category: Bouckaert J]]
-[[Category: Lahmann, M]]
+[[Category: Lahmann M]]
-[[Category: Oscarson, S]]
+[[Category: Oscarson S]]
-[[Category: Remaut, H]]
+[[Category: Remaut H]]
-[[Category: Roy, R]]
+[[Category: Roy R]]
-[[Category: Touaibia, M]]
+[[Category: Touaibia M]]
-[[Category: Vaucher, J]]
+[[Category: Vaucher J]]
-[[Category: Wellens, A]]
+[[Category: Wellens A]]
-[[Category: Bacterial adhesin]]
-[[Category: Cell adhesion]]
-[[Category: Type 1 fimbriae]]
-[[Category: Urinary tract infection]]
-[[Category: Variable immunoglobulin fold]]

4avi

From Proteopedia

Current revision

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

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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