Publication Date:
2011-06-04
Description:
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.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162478/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉 〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3162478/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉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 -- 29549/PHS HHS/ -- 48689/PHS HHS/ -- 49950/PHS HHS/ -- 85602/Medical Research Council/United Kingdom -- BB/F001134/1/Biotechnology and Biological Sciences Research Council/United Kingdom -- G0100442/Medical Research Council/United Kingdom -- G0100442(58149)/Medical Research Council/United Kingdom -- G0800002/Medical Research Council/United Kingdom -- GM62987/GM/NIGMS NIH HHS/ -- GM74985/GM/NIGMS NIH HHS/ -- P30 EB009998/EB/NIBIB NIH HHS/ -- R01 GM062987/GM/NIGMS NIH HHS/ -- England -- Nature. 2011 Jun 2;474(7349):49-53. doi: 10.1038/nature10109.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Structural and Molecular Biology, University College London and Birkbeck College, Malet Street, London WC1E 7HX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/21637253" target="_blank"〉PubMed〈/a〉
Keywords:
Adhesins, Escherichia coli/*chemistry/metabolism
;
Crystallization
;
Escherichia coli Proteins/*chemistry/metabolism
;
Fimbriae Proteins/*chemistry/metabolism
;
*Models, Molecular
;
Protein Binding
;
Protein Structure, Quaternary
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
Permalink