A1 Journal article (refereed)
1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain (2021)
Karjalainen, M., Hellman, M., Tossavainen, H., & Permi, P. (2021). 1H, 13C, and 15N NMR chemical shift assignment of the complex formed by the first EPEC EspF repeat and N-WASP GTPase binding domain. Biomolecular NMR Assignments, 15(1), 213-217. https://doi.org/10.1007/s12104-021-10008-9
JYU authors or editors
Publication details
All authors or editors: Karjalainen, Mikael; Hellman, Maarit; Tossavainen, Helena; Permi, Perttu
Journal or series: Biomolecular NMR Assignments
ISSN: 1874-2718
eISSN: 1874-270X
Publication year: 2021
Publication date: 21/01/2021
Volume: 15
Issue number: 1
Pages range: 213-217
Publisher: Springer
Publication country: Netherlands
Publication language: English
DOI: https://doi.org/10.1007/s12104-021-10008-9
Publication open access: Openly available
Publication channel open access: Partially open access channel
Publication is parallel published (JYX): https://jyx.jyu.fi/handle/123456789/73852
Abstract
LEE-encoded effector EspF (EspF) is an effector protein part of enteropathogenic Escherichia coli’s (EPEC’s) arsenal for intestinal infection. This intrinsically disordered protein contains three highly conserved repeats which together compose over half of the protein’s complete amino acid sequence. EPEC uses EspF to hijack host proteins in order to promote infection. In the attack EspF is translocated, together with other effector proteins, to host cell via type III secretion system. Inside host EspF stimulates actin polymerization by interacting with Neural Wiskott-Aldrich syndrome protein (N-WASP), a regulator in actin polymerization machinery. It is presumed that EspF acts by disrupting the autoinhibitory state of N-WASP GTPase binding domain. In this NMR spectroscopy study, we report the 1H, 13C, and 15N resonance assignments for the complex formed by the first 47-residue repeat of EspF and N-WASP GTPase binding domain. These near-complete resonance assignments provide the basis for further studies which aim to characterize structure, interactions, and dynamics between these two proteins in solution.
Keywords: proteins; NMR spectroscopy
Free keywords: EPEC EspF; intrinsically disordered protein; N-WASP; resonance assignments; solution NMR; type III secretion system
Contributing organizations
Related projects
- Conformational properties of intrinsically disordered proteins - biophysical characterization
- Permi, Perttu
- Research Council of Finland
Ministry reporting: Yes
VIRTA submission year: 2021
JUFO rating: 1