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Molecular Biophysics
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- Protein Structure and FoldingOpen Access
Donor strand sequence, rather than donor strand orientation, determines the stability and non-equilibrium folding of the type 1 pilus subunit FimA
Journal of Biological ChemistryVol. 295Issue 35p12437–12448Published online: July 10, 2020- Dawid Zyla
- Blanca Echeverria
- Rudi Glockshuber
Cited in Scopus: 2FimA is the main structural subunit of adhesive type 1 pili from uropathogenic Escherichia coli strains. Up to 3000 copies of FimA assemble to the helical pilus rod through a mechanism termed donor strand complementation, in which the incomplete immunoglobulin-like fold of each FimA subunit is complemented by the N-terminal extension (Nte) of the next subunit. The Nte of FimA, which exhibits a pseudo-palindromic sequence, is inserted in an antiparallel orientation relative to the last β-strand of the preceding subunit in the pilus.