Electric-field-stimulated protein mechanics

Article

关键词: PDZ DOMAIN;    ENERGY LANDSCAPE;    LIGAND MIGRATION;    MOLECULAR MOVIE;    GATING CHARGE;    DYNAMICS;    RECOGNITION;    BINDING;    CRYSTALLOGRAPHY;    PHOTOCYCLE;   

DOI  :  10.1038/nature20571

来源: SCIE

【 摘 要 】

The internal mechanics of proteins-the coordinated motions of amino acids and the pattern of forces constraining these motions-connects protein structure to function. Here we describe a new method combining the application of strong electric field pulses to protein crystals with time-resolved X-ray crystallography to observe conformational changes in spatial and temporal detail. Using a human PDZ domain (LNX2(PDZ2)) as a model system, we show that protein crystals tolerate electric field pulses strong enough to drive concerted motions on the sub-microsecond timescale. The induced motions are subtle, involve diverse physical mechanisms, and occur throughout the protein structure. The global pattern of electric-field-induced motions is consistent with both local and allosteric conformational changes naturally induced by ligand binding, including at conserved functional sites in the PDZ domain family. This work lays the foundation for comprehensive experimental study of the mechanical basis of protein function.

【 授权许可】

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