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dc.contributor.author
Hospenthal, Manuela
dc.contributor.author
Zyla, Dawid
dc.contributor.author
Costa, Tiago R.D.
dc.contributor.author
Redzej, Adam
dc.contributor.author
Giese, Christoph
dc.contributor.author
Lillington, James
dc.contributor.author
Glockshuber, Rudi
dc.contributor.author
Waksman, Gabriel
dc.date.accessioned
2018-11-14T09:59:12Z
dc.date.available
2017-12-16T12:10:39Z
dc.date.available
2017-12-22T13:54:17Z
dc.date.available
2018-11-14T09:59:12Z
dc.date.issued
2017-12-05
dc.identifier.other
10.1016/j.str.2017.10.004
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/221817
dc.identifier.doi
10.3929/ethz-b-000221817
dc.description.abstract
Adhesive chaperone-usher pili are long, supramolecular protein fibers displayed on the surface of many bacterial pathogens. The type 1 and P pili of uropathogenic Escherichia coli (UPEC) play important roles during urinary tract colonization, mediating attachment to the bladder and kidney, respectively. The biomechanical properties of the helical pilus rods allow them to reversibly uncoil in response to flow-induced forces, allowing UPEC to retain a foothold in the unique and hostile environment of the urinary tract. Here we provide the 4.2-Å resolution cryo-EM structure of the type 1 pilus rod, which together with the previous P pilus rod structure rationalizes the remarkable “spring-like” properties of chaperone-usher pili. The cryo-EM structure of the type 1 pilus rod differs in its helical parameters from the structure determined previously by a hybrid approach. We provide evidence that these structural differences originate from different quaternary structures of pili assembled in vivo and in vitro.
en_US
dc.language.iso
en
en_US
dc.publisher
Cell Press
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.subject
chaperone
en_US
dc.subject
pilus
en_US
dc.subject
usher
en_US
dc.subject
chaperone-usher pilus
en_US
dc.subject
type 1 pilus
en_US
dc.subject
cryo-EM
en_US
dc.subject
pilus rod
en_US
dc.subject
quaternary structure
en_US
dc.subject
FimA
en_US
dc.subject
unfolding kinetics
en_US
dc.title
The Cryoelectron Microscopy Structure of the Type 1 Chaperone-Usher Pilus Rod
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2017-11-09
ethz.journal.title
Structure
ethz.journal.volume
25
en_US
ethz.journal.issue
12
en_US
ethz.pages.start
1829
en_US
ethz.pages.end
1838.e4
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::03412 - Glockshuber, Rudolf / Glockshuber, Rudolf
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::03412 - Glockshuber, Rudolf / Glockshuber, Rudolf
ethz.date.deposited
2017-12-16T12:11:08Z
ethz.source
WOS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-12-22T13:54:21Z
ethz.rosetta.lastUpdated
2018-11-14T09:59:18Z
ethz.rosetta.exportRequired
false
ethz.rosetta.versionExported
true
ethz.COinS
ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.atitle=The%20Cryoelectron%20Microscopy%20Structure%20of%20the%20Type%201%20Chaperone-Usher%20Pilus%20Rod&rft.jtitle=Structure&rft.date=2017-12-05&rft.volume=25&rft.issue=12&rft.spage=1829&rft.epage=1838.e4&rft.au=Hospenthal,%20Manuela&Zyla,%20Dawid&Costa,%20Tiago%20R.D.&Redzej,%20Adam&Giese,%20Christoph&rft.genre=article&
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