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Title: Crystal Structure of the FimD Usher Bound to its Cognate FimC-FimH Substrate

Abstract

Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded {beta}-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the {beta}-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Lab. (BNL), Upton, NY (United States)
Sponsoring Org.:
USDOE SC OFFICE OF SCIENCE (SC)
OSTI Identifier:
1041676
Report Number(s):
BNL-97354-2012-JA
Journal ID: ISSN 0028-0836; TRN: US201212%%778
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Journal Name:
Nature
Additional Journal Information:
Journal Volume: 474; Journal Issue: 7349; Journal ID: ISSN 0028-0836
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; ADHESIVES; BACTERIA; BIOLOGY; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; POLYMERIZATION; PROTEINS; SPECTROSCOPY; SUBSTRATES; TRANSLOCATION

Citation Formats

Phan, G, Remaut, H, Wang, T, Allen, W, Pirker, K, Lebedev, A, Henderson, N, Geibel, S, Volkan, E, and et al. Crystal Structure of the FimD Usher Bound to its Cognate FimC-FimH Substrate. United States: N. p., 2011. Web. doi:10.1038/nature10109.
Phan, G, Remaut, H, Wang, T, Allen, W, Pirker, K, Lebedev, A, Henderson, N, Geibel, S, Volkan, E, & et al. Crystal Structure of the FimD Usher Bound to its Cognate FimC-FimH Substrate. United States. https://doi.org/10.1038/nature10109
Phan, G, Remaut, H, Wang, T, Allen, W, Pirker, K, Lebedev, A, Henderson, N, Geibel, S, Volkan, E, and et al. 2011. "Crystal Structure of the FimD Usher Bound to its Cognate FimC-FimH Substrate". United States. https://doi.org/10.1038/nature10109.
@article{osti_1041676,
title = {Crystal Structure of the FimD Usher Bound to its Cognate FimC-FimH Substrate},
author = {Phan, G and Remaut, H and Wang, T and Allen, W and Pirker, K and Lebedev, A and Henderson, N and Geibel, S and Volkan, E and et al.},
abstractNote = {Type 1 pili are the archetypal representative of a widespread class of adhesive multisubunit fibres in Gram-negative bacteria. During pilus assembly, subunits dock as chaperone-bound complexes to an usher, which catalyses their polymerization and mediates pilus translocation across the outer membrane. Here we report the crystal structure of the full-length FimD usher bound to the FimC-FimH chaperone-adhesin complex and that of the unbound form of the FimD translocation domain. The FimD-FimC-FimH structure shows FimH inserted inside the FimD 24-stranded {beta}-barrel translocation channel. FimC-FimH is held in place through interactions with the two carboxy-terminal periplasmic domains of FimD, a binding mode confirmed in solution by electron paramagnetic resonance spectroscopy. To accommodate FimH, the usher plug domain is displaced from the barrel lumen to the periplasm, concomitant with a marked conformational change in the {beta}-barrel. The amino-terminal domain of FimD is observed in an ideal position to catalyse incorporation of a newly recruited chaperone-subunit complex. The FimD-FimC-FimH structure provides unique insights into the pilus subunit incorporation cycle, and captures the first view of a protein transporter in the act of secreting its cognate substrate.},
doi = {10.1038/nature10109},
url = {https://www.osti.gov/biblio/1041676}, journal = {Nature},
issn = {0028-0836},
number = 7349,
volume = 474,
place = {United States},
year = {Sat Dec 31 00:00:00 EST 2011},
month = {Sat Dec 31 00:00:00 EST 2011}
}