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Dynamic mechanism for the autophosphorylation of CheA histidine kinase: molecular dynamics simulations

The two-component system (TCS) is an important signal transduction component for most bacteria. This signaling pathway is mediated by histidine kinases via autophosphorylation between P1 and P4 domains. Taking chemotaxis protein CheA as a model of TCS, the autophosphorylation mechanism of the TCS hi... Full description

Journal Title: Journal of the American Chemical Society 24 August 2005, Vol.127(33), pp.11709-19
Main Author: Zhang, Jian
Other Authors: Xu, Yechun , Shen, Jianhua , Luo, Xiaomin , Chen, Jiagao , Chen, Kaixian , Zhu, Weiliang , Jiang, Hualiang
Format: Electronic Article Electronic Article
Language: English
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ID: ISSN: 0002-7863 ; PMID: 16104748 Version:1
Link: http://pubmed.gov/16104748
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recordid: medline16104748
title: Dynamic mechanism for the autophosphorylation of CheA histidine kinase: molecular dynamics simulations
format: Article
creator:
  • Zhang, Jian
  • Xu, Yechun
  • Shen, Jianhua
  • Luo, Xiaomin
  • Chen, Jiagao
  • Chen, Kaixian
  • Zhu, Weiliang
  • Jiang, Hualiang
subjects:
  • Computer Simulation
  • Thermodynamics
  • Bacterial Proteins -- Chemistry
  • Membrane Proteins -- Chemistry
  • Protein Kinases -- Chemistry
ispartof: Journal of the American Chemical Society, 24 August 2005, Vol.127(33), pp.11709-19
description: The two-component system (TCS) is an important signal transduction component for most bacteria. This signaling pathway is mediated by histidine kinases via autophosphorylation between P1 and P4 domains. Taking chemotaxis protein CheA as a model of TCS, the autophosphorylation mechanism of the TCS histidine kinases has been investigated in this study by using a computational approach integrated homology modeling, ligand-protein docking, protein-protein docking, and molecular dynamics (MD) simulations. Four nanosecond-scale MD simulations were performed on the free P4 domain, P4-ATP, P4-TNPATP, and P1-P4-ATP complexes, respectively. Upon its binding to the binding pocket of P4 with a folded conformation, ATP gradually extends to an open state with help from a water molecule. Meanwhile, ATP forms two hydrogen bonds with His413 and Lys494 at this state. Because of the lower energy of the folded conformations, ATP shrinks back to its folded conformations, leading to the rupture of the hydrogen...
language: eng
source:
identifier: ISSN: 0002-7863 ; PMID: 16104748 Version:1
fulltext: fulltext
issn:
  • 00027863
  • 0002-7863
url: Link


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titleDynamic mechanism for the autophosphorylation of CheA histidine kinase: molecular dynamics simulations
creatorZhang, Jian ; Xu, Yechun ; Shen, Jianhua ; Luo, Xiaomin ; Chen, Jiagao ; Chen, Kaixian ; Zhu, Weiliang ; Jiang, Hualiang
ispartofJournal of the American Chemical Society, 24 August 2005, Vol.127(33), pp.11709-19
identifierISSN: 0002-7863 ; PMID: 16104748 Version:1
subjectComputer Simulation ; Thermodynamics ; Bacterial Proteins -- Chemistry ; Membrane Proteins -- Chemistry ; Protein Kinases -- Chemistry
descriptionThe two-component system (TCS) is an important signal transduction component for most bacteria. This signaling pathway is mediated by histidine kinases via autophosphorylation between P1 and P4 domains. Taking chemotaxis protein CheA as a model of TCS, the autophosphorylation mechanism of the TCS histidine kinases has been investigated in this study by using a computational approach integrated homology modeling, ligand-protein docking, protein-protein docking, and molecular dynamics (MD) simulations. Four nanosecond-scale MD simulations were performed on the free P4 domain, P4-ATP, P4-TNPATP, and P1-P4-ATP complexes, respectively. Upon its binding to the binding pocket of P4 with a folded conformation, ATP gradually extends to an open state with help from a water molecule. Meanwhile, ATP forms two hydrogen bonds with His413 and Lys494 at this state. Because of the lower energy of the folded conformations, ATP shrinks back to its folded conformations, leading to the rupture of the hydrogen...
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titleDynamic mechanism for the autophosphorylation of CheA histidine kinase: molecular dynamics simulations
descriptionThe two-component system (TCS) is an important signal transduction component for most bacteria. This signaling pathway is mediated by histidine kinases via autophosphorylation between P1 and P4 domains. Taking chemotaxis protein CheA as a model of TCS, the autophosphorylation mechanism of the TCS histidine kinases has been investigated in this study by using a computational approach integrated homology modeling, ligand-protein docking, protein-protein docking, and molecular dynamics (MD) simulations. Four nanosecond-scale MD simulations were performed on the free P4 domain, P4-ATP, P4-TNPATP, and P1-P4-ATP complexes, respectively. Upon its binding to the binding pocket of P4 with a folded conformation, ATP gradually extends to an open state with help from a water molecule. Meanwhile, ATP forms two hydrogen bonds with His413 and Lys494 at this state. Because of the lower energy of the folded conformations, ATP shrinks back to its folded conformations, leading to the rupture of the hydrogen...
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abstractThe two-component system (TCS) is an important signal transduction component for most bacteria. This signaling pathway is mediated by histidine kinases via autophosphorylation between P1 and P4 domains. Taking chemotaxis protein CheA as a model of TCS, the autophosphorylation mechanism of the TCS histidine kinases has been investigated in this study by using a computational approach integrated homology modeling, ligand-protein docking, protein-protein docking, and molecular dynamics (MD) simulations. Four nanosecond-scale MD simulations were performed on the free P4 domain, P4-ATP, P4-TNPATP, and P1-P4-ATP complexes, respectively. Upon its binding to the binding pocket of P4 with a folded conformation, ATP gradually extends to an open state with help from a water molecule. Meanwhile, ATP forms two hydrogen bonds with His413 and Lys494 at this state. Because of the lower energy of the folded conformations, ATP shrinks back to its folded conformations, leading to the rupture of the hydrogen...
pmid16104748
doi10.1021/ja051199o
eissn15205126
date2005-08-24