Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems
Abstract
Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EIsugar and NPr:EINtr, the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EIsugar interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EINtr complex was unknown. We set out to identify the key features of the interaction by performing binding assays and elucidating the structure of NPr in complex with the phosphorylation domain of EINtr (EINNtr), using a hybrid approach involving X-ray, homology, and sparse nuclear magnetic resonance. We found that the overall fold and active-site structure of the two complexes are conserved in order to maintain productive phosphorylation, however, the interface surface potential differs between the two complexes, which prevents cross-reaction.
- Authors:
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- OSTI Identifier:
- 1338976
- Resource Type:
- Journal Article
- Journal Name:
- Structure
- Additional Journal Information:
- Journal Volume: 24; Journal Issue: 12; Journal ID: ISSN 0969-2126
- Publisher:
- Elsevier
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES
Citation Formats
Strickland, Madeleine, Stanley, Ann Marie, Wang, Guangshun, Botos, Istvan, Schwieters, Charles D., Buchanan, Susan K., Peterkofsky, Alan, and Tjandra, Nico. Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. United States: N. p., 2016.
Web. doi:10.1016/j.str.2016.10.007.
Strickland, Madeleine, Stanley, Ann Marie, Wang, Guangshun, Botos, Istvan, Schwieters, Charles D., Buchanan, Susan K., Peterkofsky, Alan, & Tjandra, Nico. Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems. United States. https://doi.org/10.1016/j.str.2016.10.007
Strickland, Madeleine, Stanley, Ann Marie, Wang, Guangshun, Botos, Istvan, Schwieters, Charles D., Buchanan, Susan K., Peterkofsky, Alan, and Tjandra, Nico. 2016.
"Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems". United States. https://doi.org/10.1016/j.str.2016.10.007.
@article{osti_1338976,
title = {Structure of the NPr:EINNtr Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems},
author = {Strickland, Madeleine and Stanley, Ann Marie and Wang, Guangshun and Botos, Istvan and Schwieters, Charles D. and Buchanan, Susan K. and Peterkofsky, Alan and Tjandra, Nico},
abstractNote = {Paralogous enzymes arise from gene duplication events that confer a novel function, although it is unclear how cross-reaction between the original and duplicate protein interaction network is minimized. We investigated HPr:EIsugar and NPr:EINtr, the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EIsugar interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EINtr complex was unknown. We set out to identify the key features of the interaction by performing binding assays and elucidating the structure of NPr in complex with the phosphorylation domain of EINtr (EINNtr), using a hybrid approach involving X-ray, homology, and sparse nuclear magnetic resonance. We found that the overall fold and active-site structure of the two complexes are conserved in order to maintain productive phosphorylation, however, the interface surface potential differs between the two complexes, which prevents cross-reaction.},
doi = {10.1016/j.str.2016.10.007},
url = {https://www.osti.gov/biblio/1338976},
journal = {Structure},
issn = {0969-2126},
number = 12,
volume = 24,
place = {United States},
year = {Thu Dec 01 00:00:00 EST 2016},
month = {Thu Dec 01 00:00:00 EST 2016}
}