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

Victoria L. Robinson, David R. Buckler, Ann M. Stock

Research output: Contribution to journalReview articlepeer-review

171 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)626-633
Number of pages8
JournalNature Structural Biology
Volume7
Issue number8
DOIs
StatePublished - Aug 2000

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Genetics

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