Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation | Zendy

Ariel Méchaly | Zendy; Nathalie Sassoon | Zendy; JeanMichel Betton | Zendy; Pedro M. Alzari | Zendy

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Segmental Helical Motions and Dynamical Asymmetry Modulate Histidine Kinase Autophosphorylation

Author(s) -

Ariel Méchaly,

Nathalie Sassoon,

JeanMichel Betton,

Pedro M. Alzari

Publication year - 2014

Publication title -

plos biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 4.127

H-Index - 271

eISSN - 1545-7885

pISSN - 1544-9173

DOI - 10.1371/journal.pbio.1001776

Subject(s) - histidine kinase , autophosphorylation , biology , hamp , allosteric regulation , hamp domain , biochemistry , microbiology and biotechnology , biophysics , kinase , histidine , phosphatase , response regulator , signal transduction , phosphorylation , protein kinase a , binding site , enzyme , mutant , binding domain , hepcidin , gene , immunology , inflammation

Step-by-step structures of a prototypical E. coli histidine kinase reveal how external stimuli drive helical bending motions to control asymmetric movements of the catalytic domains.

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