Publication: Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD
Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD
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Eidam, O., Dworkowski, F. S. N., Glockshuber, R., Grütter, M. G., & Capitani, G. (2008). Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD. FEBS Letters, 582(5), 651–655. https://doi.org/10.1016/j.febslet.2008.01.030
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Abstract
Type 1 pili, anchored to the outer membrane protein FimD, enable uropathogenic Escherichia coli to attach to host cells. During pilus biogenesis, the N-terminal periplasmic domain of FimD (FimD(N)) binds complexes between the chaperone FimC and pilus subunits via its partly disordered N-terminal segment, as recently shown for the FimC-FimH(P)-FimD(N) ternary complex. We report the structure of a new ternary complex (FimC-FimF(t)-FimD(N)) with the subunit FimF(t) instead of FimH(p). FimD(N) recognizes FimC-FimF(t) and FimC-FimH(P) very
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- Eidam, O
- Dworkowski, F S N
- Glockshuber, R
- Grütter, M G
- Capitani, G
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Eidam, O., Dworkowski, F. S. N., Glockshuber, R., Grütter, M. G., & Capitani, G. (2008). Crystal structure of the ternary FimC-FimF(t)-FimD(N) complex indicates conserved pilus chaperone-subunit complex recognition by the usher FimD. FEBS Letters, 582(5), 651–655. https://doi.org/10.1016/j.febslet.2008.01.030
