sup 1^H, ^sup 15^N and ^sup 13^C resonance assignments of PpdD, a type IV pilin from enterohemorrhagic Escherichia coli

• Published in: Biomolecular NMR assignments Vol. 8; no. 1; p. 43
• Main Authors: Amorim, Gisele C, Cisneros, David A, Delepierre, Muriel, Francetic, Olivera, Izadi-pruneyre, Nadia
• Format: Journal Article
• Language: English
• Published: Dordrecht Springer Nature B.V 01.04.2014
• Subjects: Bacterial proteins; Cell adhesion & migration; E coli; Molecular biology; NMR; Nuclear magnetic resonance
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-012-9449-z

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 ^sup 1^H, ^sup 15^N and ^sup 13^C backbone and side chain resonance assignments of the C-terminal globular domain of PpdD as a first step to its structural determination.[PUBLICATION ABSTRACT]