Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate.
Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate.
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DOI:
10.1038/nature10109
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发表时间:
2011-06-02
期刊:
影响因子:
64.8
通讯作者:
Waksman, Gabriel
中科院分区:
文献类型:
--
作者:
Phan, Gilles;Remaut, Han;Wang, Tao;Allen, William J.;Pirker, Katharina F.;Lebedev, Andrey;Henderson, Nadine S.;Geibel, Sebastian;Volkan, Ender;Yan, Jun;Kunze, Micha B. A.;Pinkner, Jerome S.;Ford, Bradley;Kay, Christopher W. M.;Li, Huilin;Hultgren, Scott J.;Thanassi, David G.;Waksman, Gabriel
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 catalyzes their polymerization and mediates pilus translocation across the outer membrane. 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 β-barrel translocation channel. FimC:FimH is held in place through interactions with the two C-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 dramatic conformational change in the β-barrel. The N-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.
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DOI:
10.1107/s0907444905036693
发表时间:
2006-01-01
影响因子:
2.2
作者:
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影响因子:
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