9q1v | pdb_00009q1v

Crystal Structure of de novo design FimH minibinder F7 complex

spinqualitylabelsall models 9q1v, resolution 1.75Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 9q1v is a 4 chain structure with sequence from Escherichia coli and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.75Å 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 The rise of multidrug-resistant bacterial infections necessitates the discovery of novel antimicrobial strategies. Here, we show that protein design provides a generalizable means of generating new antimicrobials by neutralizing the function of bacterial adhesins, which are virulence factors critical in host-pathogen interactions. We de novo designed high-affinity miniprotein binders to FimH and Abp1D/Abp2D chaperone usher pili adhesins from uropathogenic Escherichia coli and Acinetobacter baumannii, respectively, which are implicated in mediating both uncomplicated and catheter-associated urinary tract infections (UTI) responsible for significant morbidity and mortality worldwide. The designed antagonists have high specificity and stability, disrupt bacterial recognition of host receptors, block biofilm formation, and are effective in treating and preventing uncomplicated and catheter-associated UTIs in vivo. Targeting virulence factors outside the cell membrane with protein design provides a rapid route to next-generation therapeutics that can disrupt pathogenesis and thus are capable of treating and preventing disease in an antibiotic-sparing manner. De Novo Design of Miniprotein Inhibitors of Bacterial Adhesins.,Chazin-Gray AM, Thompson TR, Lopatto EDB, Magala P, Erickson PW, Hunt AC, Manchenko A, Aprikian P, Tchesnokova V, Basova I, Sanick DA, Tamadonfar KO, Timm MR, Pinkner JS, Dodson KW, Kang A, Joyce E, Bera AK, Schmitz AJ, Ellebedy AH, Hvorecny KL, Cartwright MJ, Vernet A, Bardales S, White D, Klevit RE, Sokurenko EV, Hultgren SJ, Baker D bioRxiv [Preprint]. 2025 Aug 18:2025.08.18.670751. doi: , 10.1101/2025.08.18.670751. PMID:40894640 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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