Journal
STRUCTURE
Volume 24, Issue 12, Pages 2127-2137Publisher
CELL PRESS
DOI: 10.1016/j.str.2016.10.007
Keywords
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Funding
- Intramural Research Programs of the NHLBI at the NIH
- NIDDK at the NIH
- CIT at the NIH
- Eppley Institute at the University of Nebraska Medical Center
- US Department of Energy, Office of Science, Office of Basic Energy Sciences [W-31-109-Eng-38]
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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.
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