Biological insights from structures of two-component proteins

Rong Gao, Ann Stock

Research output: Contribution to journalReview article

446 Scopus citations


Two-component signal transduction based on phosphotransfer from a histidine protein kinase to a response regulator protein is a prevalent strategy for coupling environmental stimuli to adaptive responses in bacteria. In both histidine kinases and response regulators, modular domains with conserved structures and biochemical activities adopt different conformational states in the presence of stimuli or upon phosphorylation, enabling a diverse array of regulatory mechanisms based on inhibitory and/or activating protein-protein interactions imparted by different domain arrangements. This review summarizes some of the recent structural work that has provided insight into the functioning of bacterial histidine kinases and response regulators. Particular emphasis is placed on identifying features that are expected to be conserved among different two-component proteins from those that are expected to differ, with the goal of defining the extent to which knowledge of previously characterized two-component proteins can be applied to newly discovered systems.

Original languageEnglish (US)
Pages (from-to)133-154
Number of pages22
JournalAnnual Review of Microbiology
StatePublished - Oct 1 2009

All Science Journal Classification (ASJC) codes

  • Microbiology


  • Histidine kinase
  • Phosphorylation
  • Phosphotransfer
  • Response regulator
  • Signal transduction

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