Visualizing an ultra-weak protein-protein interaction in phosphorylation signaling.

Autor: Xing Q; CAS Key Laboratory of Magnetic Resonance in Biological Systems, Wuhan Center for Magnetic Resonance, State Key Laboratory of Magnetic Resonance and Atomic Molecular Physics, Wuhan Institute of Physics and Mathematics of the Chinese Academy of Sciences, Xiao-Hong Shan, Wuhan, Hubei 430071 (China) http://tanglab.wipm.ac.cn., Huang P, Yang J, Sun JQ, Gong Z, Dong X, Guo DC, Chen SM, Yang YH, Wang Y, Yang MH, Yi M, Ding YM, Liu ML, Zhang WP, Tang C
Jazyk: angličtina
Zdroj: Angewandte Chemie (International ed. in English) [Angew Chem Int Ed Engl] 2014 Oct 20; Vol. 53 (43), pp. 11501-5. Date of Electronic Publication: 2014 Aug 11.
DOI: 10.1002/anie.201405976
Abstrakt: 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.
(© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.)
Databáze: MEDLINE
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