The ArcB Sensor Kinase of
            <i>Escherichia coli</i>
            Autophosphorylates by an Intramolecular Reaction

Peña-Sandoval, Gabriela R.; Georgellis, Dimitris

doi:10.1128/jb.01401-09

Cited by 40 publications

(49 citation statements)

References 37 publications

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“…Experimental evidence for the trans-phosphorylation mechanism in the NrII and EnvZ kinases is strong (33,34). Only recently has this trans-paradigm been challenged by the observation that some kinases phosphorylate in cis, including HK853 (8,35). The notion that different phosphorylation mechanisms exist among the set of HisKA-type sensor kinases is seemingly at odds with the notion that interaction residue contacts defining inactive and active states of the kinase can be extracted from HisKA-HATPase_c sequence databases.…”

Section: Discussionmentioning

confidence: 65%

Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis

Dago

Schug

Procaccini

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

137

139

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Signal transduction proteins such as bacterial sensor histidine kinases, designed to transition between multiple conformations, are often ruled by unstable transient interactions making structural characterization of all functional states difficult. This study explored the inactive and signal-activated conformational states of the two catalytic domains of sensor histidine kinases, HisKA and HATPase. Direct coupling analyses, a global statistical inference approach, was applied to >13,000 such domains from protein databases to identify residue contacts between the two domains. These contacts guided structural assembly of the domains using MAGMA, an advanced molecular dynamics docking method. The active conformation structure generated by MAGMA simultaneously accommodated the sequence derived residue contacts and the ATP-catalytic histidine contact. The validity of this structure was confirmed biologically by mutation of contact positions in the Bacillus subtilis sensor histidine kinase KinA and by restoration of activity in an inactive KinA(HisKA):KinD(HATPase) hybrid protein.These data indicate that signals binding to sensor domains activate sensor histidine kinases by causing localized strain and unwinding at the end of the C-terminal helix of the HisKA domain. This destabilizes the contact positions of the inactive conformation of the two domains, identified by previous crystal structure analyses and by the sequence analysis described here, inducing the formation of the active conformation. This study reveals that structures of unstable transient complexes of interacting proteins and of protein domains are accessible by applying this combination of crossvalidating technologies.coevolution | signal transduction | two component system | protein structure prediction | biological physics P rotein-protein interaction is the essence of signal transduction and essential for protein function at all levels of life. Proteins are frequently required to undergo conformational transitions between multiple states characterized by unique transient residue interactions for each state. Attempts to describe features of these states depend upon techniques that investigate single molecules at sub-ms timescales (1), mechanically pull them (2), or quantify their dynamics (3). On the theoretical side, energy landscape theory provides a basis to understand protein folding and function (4), and atomically resolved simulations can describe transitions between multiple (native) conformations covering ms timescales on specialized supercomputers (5).Yet, despite all these advances, a full structural characterization of multiple conformations for a specific system remains a daunting task. Some states, active states in particular, are intrinsically short-lived and therefore difficult to stabilize for direct measurements or capture in a crystal lattice. By utilizing a strategy of integrating information from cross-disciplinary approaches, we show here that the shortcomings of individual techniques may be circumvented. By doing so, we introdu...

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Section: Discussionmentioning

confidence: 65%

Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis

Dago

Schug

Procaccini

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

137

139

View full text Add to dashboard Cite

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“…Similar studies on the structurally distinct CheA chemotaxis kinase also demonstrated a trans-mechanism supporting the notion that perhaps all HK phosphorylate in trans [80]. This notion was not challenged until several laboratories showed cis phosphorylation in HK, e.g., the structurally resolved Thermotoga maritima kinase HK853 [81] and E.coli kinase ArcB [82]. …”

Section: Kinase Activationmentioning

confidence: 79%

Molecular Mechanisms of Two-Component Signal Transduction

Zschiedrich

Keidel

Szurmant

2016

Journal of Molecular Biology

455

364

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Two-component systems comprising sensor histidine kinases and response regulator proteins are among the most important players in bacterial and archaeal signal transduction and also occur in reduced numbers in some eukaryotic organisms. Given their importance to cellular survival, virulence and cellular development these systems are among the most scrutinized bacterial proteins. In recent years a flurry of bioinformatics, genetic, biochemical and structural studies have provided detailed insights into many of the molecular mechanisms that underlie the detection of signals and the generation of the appropriate response by two-component systems. Importantly, it has become clear that there is significant diversity in the mechanisms employed by individual systems. This review discusses the current knowledge on common themes and divergences from the paradigm of two-component system signaling. An emphasis is on the information gained by a flurry of recent structural and bioinformatics studies.

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“…That is, the gamma-phosphoryl group of ATP, which is bound to one monomer in the homodimer, is transferred to the other monomer. On the contrary, it has been recently proposed that ArcB autophosphorylates through an intramolecular and not through an intermolecular reaction as previously proposed (175).…”

Section: Redox Control Of the Adaptation Of Aerobic Respiration mentioning

confidence: 87%

Bacterial Adaptation of Respiration from Oxic to Microoxic and Anoxic Conditions: Redox Control

Cendejas-Bueno

Mesa

Bedmar

et al. 2012

Antioxidants & Redox Signaling

155

148

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Under a shortage of oxygen, bacterial growth can be faced mainly by two ATP-generating mechanisms: (i) by synthesis of specific high-affinity terminal oxidases that allow bacteria to use traces of oxygen or (ii) by utilizing other substrates as final electron acceptors such as nitrate, which can be reduced to dinitrogen gas through denitrification or to ammonium. This bacterial respiratory shift from oxic to microoxic and anoxic conditions requires a regulatory strategy which ensures that cells can sense and respond to changes in oxygen tension and to the availability of other electron acceptors. Bacteria can sense oxygen by direct interaction of this molecule with a membrane protein receptor (e.g., FixL) or by interaction with a cytoplasmic transcriptional factor (e.g., Fnr). A third type of oxygen perception is based on sensing changes in redox state of molecules within the cell. Redox-responsive regulatory systems (e.g., ArcBA, RegBA/PrrBA, RoxSR, RegSR, ActSR, ResDE, and Rex) integrate the response to multiple signals (e.g., ubiquinone, menaquinone, redox active cysteine, electron transport to terminal oxidases, and NAD/NADH) and activate or repress target genes to coordinate the adaptation of bacterial respiration from oxic to anoxic conditions. Here, we provide a compilation of the current knowledge about proteins and regulatory networks involved in the redox control of the respiratory adaptation of different bacterial species to microxic and anoxic environments.

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The ArcB Sensor Kinase of Escherichia coli Autophosphorylates by an Intramolecular Reaction

Cited by 40 publications

References 37 publications

Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis

Structural basis of histidine kinase autophosphorylation deduced by integrating genomics, molecular dynamics, and mutagenesis

Molecular Mechanisms of Two-Component Signal Transduction

Bacterial Adaptation of Respiration from Oxic to Microoxic and Anoxic Conditions: Redox Control

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