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- PDB-5jqi: Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5jqi | ||||||
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Title | Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N-terminal extension | ||||||
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![]() | SUGAR BINDING PROTEIN / lectin / immunoglobulin fold / carbohydrate binding protein / donor strand exchange | ||||||
Function / homology | ![]() cell adhesion involved in single-species biofilm formation / pilus / cell adhesion Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Kalas, V. / Hultgren, S.J. | ||||||
![]() | ![]() Title: Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. Authors: Vasilios Kalas / Jerome S Pinkner / Thomas J Hannan / Michael E Hibbing / Karen W Dodson / Alex S Holehouse / Hao Zhang / Niraj H Tolia / Michael L Gross / Rohit V Pappu / James Janetka / Scott J Hultgren / ![]() Abstract: Positive selection in the two-domain type 1 pilus adhesin FimH enhances fitness in urinary tract infection (UTI). We report a comprehensive atomic-level view of FimH in two-state conformational ...Positive selection in the two-domain type 1 pilus adhesin FimH enhances 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. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 240.9 KB | Display | ![]() |
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PDB format | ![]() | 193.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5jr4C ![]() 3jwnS C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein/peptide | Mass: 1513.776 Da / Num. of mol.: 4 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() #2: Protein | Mass: 29053.260 Da / Num. of mol.: 4 / Fragment: UNP residues 22-300 / Mutation: A62S Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: UTI89 / UPEC / Gene: fimH, UTI89_C5017 / Production host: ![]() ![]() #3: Chemical | ChemComp-GOL / #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.36 Å3/Da / Density % sol: 47.94 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop Details: 0.2 M Calcium Acetate, 0.1 M HEPES 7.5, 10% PEG 8000 PH range: 5-8 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 21, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→48.67 Å / Num. obs: 75411 / % possible obs: 94.2 % / Redundancy: 3.9 % / Rmerge(I) obs: 0.141 / Net I/σ(I): 8.5 |
Reflection shell | Resolution: 1.96→2.03 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.706 / Mean I/σ(I) obs: 2 / % possible all: 90.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3JWN Resolution: 1.962→48.666 Å / SU ML: 0.25 / Cross valid method: FREE R-VALUE / σ(F): 1.96 / Phase error: 25.08
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.962→48.666 Å
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Refine LS restraints |
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LS refinement shell |
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