ArticleJournal of molecular biology2008
Determination of the physiological dimer interface of the PhoQ sensor domain.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- The PhoPQ two-component regulatory system as an important regulator of bacterial stress response.Molecular biology reports · 2025Review
- Atomic insights into the signaling landscape of E. coli PhoQ histidine kinase from molecular dynamics simulations.Scientific reports · 2024Article
- Multistep Signaling in Nature: A Close-Up ofInternational journal of molecular sciences · 2021Review
- Disentangling constraints using viability evolution principles in integrative modeling of macromolecular assemblies.Scientific reports · 2017Article
- Design and engineering of artificial oxygen-activating metalloenzymes.Chemical Society reviews · 2016Review
- Cys-scanning disulfide crosslinking and bayesian modeling probe the transmembrane signaling mechanism of the histidine kinase, PhoQ.Structure (London, England : 1993) · 2014Article
- The histidine kinase CusS senses silver ions through direct binding by its sensor domain.Biochimica et biophysica acta · 2014Article
- Assembly of the transmembrane domain of E. coli PhoQ histidine kinase: implications for signal transduction from molecular simulations.PLoS computational biology · 2013Article
- The integrity of the periplasmic domain of the VirA sensor kinase is critical for optimal coordination of the virulence signal response in Agrobacterium tumefaciens.Journal of bacteriology · 2011Article
- Probing designability via a generalized model of helical bundle geometry.Journal of molecular biology · 2011Article
- FeuN, a novel modulator of two-component signalling identified in Sinorhizobium meliloti.Molecular microbiology · 2010Article
- Transmembrane polar interactions are required for signaling in the Escherichia coli sensor kinase PhoQ.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Feedback inhibition in the PhoQ/PhoP signaling system by a membrane peptide.PLoS genetics · 2009Article
- Biological insights from structures of two-component proteins.Annual review of microbiology · 2009Article
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Authors and funding
4 authors.
Funding
Abstract
PhoQ is the transmembrane sensor kinase of the phoPQ two-component system, which detects and responds to divalent cations and antimicrobial peptides and can trigger bacterial virulence. Despite their ubiquity and importance in bacterial signaling, the structure and molecular mechanism of the sensor kinases is not fully understood. Frequently, signals are transmitted from a periplasmic domain in these proteins to the cytoplasmic kinase domains via an extended dimeric interface, and the PhoQ protein would appear to follow this paradigm. However, the isolated truncated periplasmic domain of PhoQ dimerizes poorly, so it has been difficult to distinguish the relevant interface in crystal structures of the PhoQ periplasmic domain. Thus, to determine the arrangement of the periplasmic domains of Escherichia coli PhoQ in the physiological homodimer, disulfide-scanning mutagenesis was used. Single cysteine substitutions were introduced along the N-terminal helix of the periplasmic region, and the degree of cross-linking in each protein variant was determined by Western blotting and immunodetection. The results were subjected to periodicity analysis to generate a profile that provides information concerning the C(beta) distances between corresponding residues at the interface. This profile, together with a rigid-body search procedure, side-chain placement, and energy minimization, was used to build a model of the dimer arrangement. The final model proved to be highly compatible with one of the PhoQ crystal structures, 3BQ8, indicating that 3BQ8 is representative of the physiological arrangement. The model of the periplasmic region is also compatible with a full-length PhoQ protein in which a four-helix bundle forms in the membrane. The membrane four-helix bundle has been proposed for other sensor kinases and is thought to have a role in the mechanism of signal transduction; our model supports the idea that signaling through a membrane four-helix bundle is a widespread mechanism in the transmembrane sensor kinases.
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