NDLI: Complete $^{1}$H, $^{13}$C and $^{15}$N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli

Content Provider	Springer Nature Link
Author	Yang, Yi Berry, Andrea A. Lee, Wei Chao Garnett, James A. Marchant, Jan Levine, Jonathan A. Simpson, Peter J. Fogel, Sarah A. Varney, Kristen M. Matthews, Steven J. Nataro, James P. Inman, Keith G.
Copyright Year	2010
Abstract	Aggregative adherence fimbriae (AAF) are the primary adhesive factors of enteroaggregative Escherichia coli (EAEC) and are required for intestinal colonization. They mediate binding to extracellular matrix proteins of the enteric mucosa and display proinflammatory effects on epithelial cells in vitro. Among the simplest of bacterial fimbriae, these passive hairlike appendages are composed primarily of a single 16-kDa structural and adhesive subunit, AafA. Oligomerization occurs by incorporating the N-terminal strand of each AafA subunit into an otherwise incomplete β-sheet of an adjacent AafA subunit. We have engineered a highly soluble AafA monomer by positioning the N-terminal “donor strand” at the C-terminus, following a turn and short linker that were introduced to allow access of the donor strand to the recipient cleft of the same subunit. The resulting “donor-strand complemented” AafA subunit, or AafA-dsc folds autonomously, is monodisperse in solution, and yields high quality NMR spectral data. Here, we report the $^{1}$H, $^{13}$C, and $^{15}$N chemical shift assignments for AafA-dsc.
Starting Page	1
Ending Page	5
Page Count	5
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	5
Issue Number	1
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2010-08-17
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	AafA Aggregative adherence fimbriae Adhesin Donor strand Enteroaggregative NMR resonance assignment Biochemistry Biophysics and Biological Physics Polymer Sciences
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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