5JQI
Crystal structure of FimH A62S from E. coli UTI89 bound to FimG N-terminal extension
Summary for 5JQI
| Entry DOI | 10.2210/pdb5jqi/pdb |
| Related | 5JR4 |
| Descriptor | FimG N-terminal extension, Type 1 fimbiral adhesin FimH, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | lectin, immunoglobulin fold, carbohydrate binding protein, sugar binding protein, donor strand exchange |
| Biological source | Escherichia coli (strain UTI89 / UPEC) More |
| Total number of polymer chains | 8 |
| Total formula weight | 122636.52 |
| Authors | Kalas, V.,Hultgren, S.J. (deposition date: 2016-05-05, release date: 2017-02-22, Last modification date: 2024-10-23) |
| Primary citation | Kalas, V.,Pinkner, J.S.,Hannan, T.J.,Hibbing, M.E.,Dodson, K.W.,Holehouse, A.S.,Zhang, H.,Tolia, N.H.,Gross, M.L.,Pappu, R.V.,Janetka, J.,Hultgren, S.J. Evolutionary fine-tuning of conformational ensembles in FimH during host-pathogen interactions. Sci Adv, 3:e1601944-e1601944, 2017 Cited by PubMed 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 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. PubMed: 28246638DOI: 10.1126/sciadv.1601944 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.962 Å) |
Structure validation
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