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5jqi
From Proteopedia
(Difference between revisions)
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<StructureSection load='5jqi' size='340' side='right' caption='[[5jqi]], [[Resolution|resolution]] 1.96Å' scene=''> | <StructureSection load='5jqi' size='340' side='right' caption='[[5jqi]], [[Resolution|resolution]] 1.96Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5jqi]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jqi]] is a 8 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=5JQI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JQI FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jr4|5jr4]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jr4|5jr4]]</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqi OCA], [http://pdbe.org/5jqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqi RCSB], [http://www.ebi.ac.uk/pdbsum/5jqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqi 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=5jqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jqi OCA], [http://pdbe.org/5jqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jqi RCSB], [http://www.ebi.ac.uk/pdbsum/5jqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jqi ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:28246638</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jqi" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Adhesin|Adhesin]] | *[[Adhesin|Adhesin]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Ecout]] | ||
[[Category: Hultgren, S J]] | [[Category: Hultgren, S J]] | ||
[[Category: Kalas, V]] | [[Category: Kalas, V]] | ||
Revision as of 06:23, 18 April 2018
Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N-terminal extension
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