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Nat Struct Biol. 2000 Aug;7(8):626-33.

A tale of two components: a novel kinase and a regulatory switch.

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Center for Advanced Biotechnology and Medicine and Department of Biochemistry, UMDNJ-Robert Wood Johnson Medical School, 679 Hoes Lane, Piscataway, New Jersey 08854-5627, USA.


Histidine protein kinases and response regulators form the basis of phosphotransfer signal transduction pathways. Commonly referred to as two-component systems, these modular and adaptable signaling schemes are prevalent in prokaryotes. Structures of the core domains of histidine kinases reveal a protein kinase fold different from that of the Ser/Thr/Tyr protein kinase family, but similar to that of other ATP binding domains. Recent structure determinations of phosphorylated response regulator domains indicate a conserved mechanism for the propagated conformational change that accompanies phosphorylation of an active site Asp residue. The altered molecular surface promotes specific protein-protein interactions that mediate the downstream response.

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