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| | ==Crystal structure of FimH A27V/V163A from E. coli UTI89 bound to FimG N-terminal extension== | | ==Crystal structure of FimH A27V/V163A from E. coli UTI89 bound to FimG N-terminal extension== |
| - | <StructureSection load='5jr4' size='340' side='right' caption='[[5jr4]], [[Resolution|resolution]] 2.60Å' scene=''> | + | <StructureSection load='5jr4' size='340' side='right'caption='[[5jr4]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jr4]] 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=5JR4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JR4 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jr4]] 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=5JR4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JR4 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.596Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jqi|5jqi]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">fimH, UTI89_C5017 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=364106 ECOUT])</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=5jr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jr4 OCA], [https://pdbe.org/5jr4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jr4 RCSB], [https://www.ebi.ac.uk/pdbsum/5jr4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jr4 ProSAT]</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=5jr4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jr4 OCA], [http://pdbe.org/5jr4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jr4 RCSB], [http://www.ebi.ac.uk/pdbsum/5jr4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jr4 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q1R2J4_ECOUT Q1R2J4_ECOUT] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Adhesin|Adhesin]] | + | *[[Adhesin 3D structures|Adhesin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecout]] | + | [[Category: Escherichia coli UTI89]] |
| - | [[Category: Hultgren, S J]] | + | [[Category: Large Structures]] |
| - | [[Category: Kalas, V]] | + | [[Category: Hultgren SJ]] |
| - | [[Category: Carbohydrate binding protein]] | + | [[Category: Kalas V]] |
| - | [[Category: Donor strand exchange]]
| + | |
| - | [[Category: Immunoglobulin fold]]
| + | |
| - | [[Category: Lectin]]
| + | |
| - | [[Category: Sugar binding protein]]
| + | |
| Structural highlights
Function
Q1R2J4_ECOUT
Publication Abstract from PubMed
Positive selection in the two-domain type 1 pilus adhesin FimH enhances Escherichia coli fitness in urinary tract infection (UTI). We report a comprehensive atomic-level view of FimH in two-state conformational ensembles in solution, composed of one low-affinity tense (T) and multiple high-affinity relaxed (R) conformations. Positively selected residues allosterically modulate the equilibrium between these two conformational states, each of which engages mannose through distinct binding orientations. A FimH variant that only adopts the R state is severely attenuated early in a mouse model of uncomplicated UTI but is proficient at colonizing catheterized bladders in vivo or bladder transitional-like epithelial cells in vitro. Thus, the bladder habitat has barrier(s) to R state-mediated colonization possibly conferred by the terminally differentiated bladder epithelium and/or decoy receptors in urine. Together, our studies reveal the conformational landscape in solution, binding mechanisms, and adhesive strength of an allosteric two-domain adhesin that evolved "moderate" affinity to optimize persistence in the bladder during UTI.
Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions.,Kalas V, Pinkner JS, Hannan TJ, Hibbing ME, Dodson KW, Holehouse AS, Zhang H, Tolia NH, Gross ML, Pappu RV, Janetka J, Hultgren SJ Sci Adv. 2017 Feb 10;3(2):e1601944. doi: 10.1126/sciadv.1601944. eCollection 2017, Feb. PMID:28246638[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kalas V, Pinkner JS, Hannan TJ, Hibbing ME, Dodson KW, Holehouse AS, Zhang H, Tolia NH, Gross ML, Pappu RV, Janetka J, Hultgren SJ. Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. Sci Adv. 2017 Feb 10;3(2):e1601944. doi: 10.1126/sciadv.1601944. eCollection 2017, Feb. PMID:28246638 doi:http://dx.doi.org/10.1126/sciadv.1601944
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