5T1N

Solution-state NMR structural ensemble of NPr (1-85) refined with RDCs and PCS

Summary for 5T1N

• Entry DOI: 10.2210/pdb5t1n/pdb
• NMR Information: BMRB: 30158
• Descriptor: Phosphocarrier protein NPr (1 entity in total)
• Functional Keywords: ptsntr, phosphotransfer, hpr-like, bacterial, transferase
• Biological source: Escherichia coli O157:H7
• Total number of polymer chains: 1
• Total formula weight: 9254.57

Authors

Strickland, M.,Wang, G.,Peterkofsky, A.,Tjandra, N. (deposition date: 2016-08-19, release date: 2016-11-16, Last modification date: 2024-05-01)

Primary citation

Strickland, M.,Stanley, A.M.,Wang, G.,Botos, I.,Schwieters, C.D.,Buchanan, S.K.,Peterkofsky, A.,Tjandra, N.
Structure of the NPr:EIN(Ntr) Complex: Mechanism for Specificity in Paralogous Phosphotransferase Systems.
Structure, 24:2127-2137, 2016

PubMed 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:EI and NPr:EI, the initial complexes of paralogous phosphorylation cascades involved in sugar import and nitrogen regulation in bacteria, respectively. Although the HPr:EI interaction has been well characterized, involving multiple complexes and transient interactions, the exact nature of the NPr:EI 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 EI (EIN), 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.

PubMed: 27839951
DOI: 10.1016/j.str.2016.10.007

Experimental method

SOLUTION NMR