2MP0

Protein Phosphorylation upon a Fleeting Encounter

Summary for 2MP0

• Entry DOI: 10.2210/pdb2mp0/pdb
• NMR Information: BMRB: 19958
• Descriptor: Phosphoenolpyruvate-protein phosphotransferase, Glucose-specific phosphotransferase enzyme IIA component, PHOSPHITE ION (3 entities in total)
• Functional Keywords: ein eiiaglc complex, transferase
• Biological source: Escherichia coli; More
• Total number of polymer chains: 2
• Total formula weight: 46444.93

Authors

Xing, Q.,Yang, J.,Huang, P.,Zhang, W.,Tang, C. (deposition date: 2014-05-08, release date: 2014-08-20, Last modification date: 2024-05-01)

Primary citation

Xing, Q.,Huang, P.,Yang, J.,Sun, J.Q.,Gong, Z.,Dong, X.,Guo, D.C.,Chen, S.M.,Yang, Y.H.,Wang, Y.,Yang, M.H.,Yi, M.,Ding, Y.M.,Liu, M.L.,Zhang, W.P.,Tang, C.
Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling.
Angew.Chem.Int.Ed.Engl., 53:11501-11505, 2014

PubMed Abstract: Proteins interact with each other to fulfill their functions. The importance of weak protein-protein interactions has been increasingly recognized. However, owing to technical difficulties, ultra-weak interactions remain to be characterized. Phosphorylation can take place via a K(D)≈25 mM interaction between two bacterial enzymes. Using paramagnetic NMR spectroscopy and with the introduction of a novel Gd(III)-based probe, we determined the structure of the resulting complex to atomic resolution. The structure accounts for the mechanism of phosphoryl transfer between the two enzymes and demonstrates the physical basis for their ultra-weak interaction. Further, molecular dynamics (MD) simulations suggest that the complex has a lifetime in the micro- to millisecond regimen. Hence such interaction is termed a fleeting interaction. From mathematical modeling, we propose that an ultra-weak fleeting interaction enables rapid flux of phosphoryl signal, providing a high effective protein concentration.

PubMed: 25131700
DOI: 10.1002/anie.201405976

Experimental method

SOLUTION NMR