Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

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

1H, 15N and 13C resonance assignments of PpdD, a type IV pilin from enterohemorrhagic Escherichia... 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 1H, 15N and 13C backbone and side chain resonance assignments of the C-terminal globular domain of PpdD as a first step to its structural determination. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals

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

Loading next page...
 
/lp/springer-journals/1h-15n-and-13c-resonance-assignments-of-ppdd-a-type-iv-pilin-from-zPxm0jR0d4

References (20)

Publisher
Springer Journals
Copyright
Copyright © 2012 by Springer Science+Business Media Dordrecht
Subject
Physics; Biophysics and Biological Physics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
DOI
10.1007/s12104-012-9449-z
pmid
23242787
Publisher site
See Article on Publisher Site

Abstract

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

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Dec 15, 2012

There are no references for this article.