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Biological Insights from Structures of Two-Component Proteins

Open access
Gao, Rong, Stock, Ann M.·2009·Annual Review of Microbiology

Abstract

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.

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Crossref · 10.1146/annurev.micro.091208.073214

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Metadata

Authors
Gao, R., & Stock, A. M.
Venue
Annual Review of Microbiology
Published
2009-10-01
Volume
63
Issue
1
Pages
133-154
ISSN
  • 0066-4227 (ISSN-L)
  • 1545-3251
OpenAlex
W2125112034
Cited by
792
References
2
FWCI
3.75
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Biological Insights from Structures of Two-Component Proteins. https://app.cochat.ai/papers/10.1146/annurev.micro.091208.073214
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Gao, R., & Stock, A. M. (2009). Biological Insights from Structures of Two-Component Proteins. Annual Review of Microbiology. https://doi.org/10.1146/annurev.micro.091208.073214

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.