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¹H, ¹⁵N and ¹³C resonance assignments of PpdD, a type IV pilin from enterohemorrhagic Escherichia coli
Unité de Génétique Moléculaire, Département de MicrobiologieInstitut Pasteur, Paris Cedex 15 France; CNRS, ERL 3526, Paris, France.ORCID iD: 0000-0001-9919-0075
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2014 (English)In: Biomolecular NMR Assignments, ISSN 1874-2718, E-ISSN 1874-270X, Vol. 8, no 1, p. 43-46Article in journal (Refereed) Published
Abstract [en]

Bacterial type 4 pili (T4P) are long flexible fibers involved in adhesion, DNA uptake, phage transduction, aggregation and a flagella-independent movement called "twitching motility". T4P comprise thousands of copies of the major pilin subunit, which is initially inserted in the plasma membrane, processed and assembled into dynamic helical filaments. T4P are crucial for host colonization and virulence of many Gram-negative bacteria. In enterohemorrhagic Escherichia coli the T4P, called hemorrhagic coli pili (HCP) promote cell adhesion, motility, biofilm formation and signaling. To understand the mechanism of HCP assembly and function, we analyzed the structure of the major subunit prepilin peptidase-dependent protein D (PpdD) (also called HcpA), a 15 kDa pilin with two potential disulfide bonds. Here we present the (1)H, (15)N and (13)C backbone and side chain resonance assignments of the C-terminal globular domain of PpdD as a first step to its structural determination.

Place, publisher, year, edition, pages
2014. Vol. 8, no 1, p. 43-46
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Infectious Medicine Microbiology
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URN: urn:nbn:se:umu:diva-156769DOI: 10.1007/s12104-012-9449-zPubMedID: 23242787OAI: oai:DiVA.org:umu-156769DiVA, id: diva2:1291978
Available from: 2019-02-26 Created: 2019-02-26 Last updated: 2019-03-08Bibliographically approved

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Cisneros, David A.

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