Engineering an Osmosensor by Pivotal Histidine Positioning within Disordered Helices

Madhubrata Ghosh, Loo Chien Wang, Roland G. Huber, Yunfeng Gao, Leslie K. Morgan, Nikhil Kumar Tulsian, Peter J. Bond, Linda Kenney, Ganesh S. Anand

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

A His-Asp/Glu dyad forms the core of EnvZ histidine kinase (HK) osmosensing wherein osmolytes mediate changes in the backbone and side-chain microenvironment, leading to enhanced histidine autophosphorylation. This His-Asp/Glu dyad is highly conserved across diverse HKs, suggesting a unified model for integrating diverse environmental stimuli to a singular histidine phosphorylation response.

Original languageEnglish (US)
Pages (from-to)302-314.e4
JournalStructure
Volume27
Issue number2
DOIs
StatePublished - Feb 5 2019
Externally publishedYes

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Keywords

  • amide hydrogen-deuterium exchange mass spectrometry
  • EnvZ
  • H bonding
  • helix stabilization
  • His-Asp/Glu dyad
  • histidine rotamerization
  • osmosensing
  • protein dynamics
  • two-component signal transduction

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Cite this

Ghosh, M., Wang, L. C., Huber, R. G., Gao, Y., Morgan, L. K., Tulsian, N. K., Bond, P. J., Kenney, L., & Anand, G. S. (2019). Engineering an Osmosensor by Pivotal Histidine Positioning within Disordered Helices. Structure, 27(2), 302-314.e4. https://doi.org/10.1016/j.str.2018.10.012