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- PDB-9m08: Structure of outer membrane lipoprotein QseG and histidine kinase... -

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Basic information

Entry
Database: PDB / ID: 9m08
TitleStructure of outer membrane lipoprotein QseG and histidine kinase QseE complex
Components
  • Quorum-sensing regulator protein G
  • histidine kinase
KeywordsSIGNALING PROTEIN / complex
Function / homology
Function and homology information


osmosensory signaling via phosphorelay pathway / phosphorelay response regulator activity / phosphorelay sensor kinase activity / histidine kinase / protein kinase activator activity / ATP binding / plasma membrane
Similarity search - Function
Quorum-sensing regulator protein G / YfhG lipoprotein / : / Histidine kinase/HSP90-like ATPase / His Kinase A (phospho-acceptor) domain / His Kinase A (phosphoacceptor) domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase-related protein, C-terminal / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Histidine kinase domain ...Quorum-sensing regulator protein G / YfhG lipoprotein / : / Histidine kinase/HSP90-like ATPase / His Kinase A (phospho-acceptor) domain / His Kinase A (phosphoacceptor) domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase-related protein, C-terminal / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Histidine kinase domain / Histidine kinase domain profile. / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase superfamily
Similarity search - Domain/homology
Hypothetical membrane protein / histidine kinase
Similarity search - Component
Biological speciesSalmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (bacteria)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsGao, X. / Li, G.B. / Gong, P.Q.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32200144 China
CitationJournal: mBio / Year: 2025
Title: Cryo-EM structure of the QseG-QseE complex reveals an accessory protein-driven two-component system activation mechanism.
Authors: Piqian Gong / Guobang Li / Weixun Li / Mengyuan Xu / Xuyao Jiao / Xudong Chen / Beile Gao / Xiang Gao /
Abstract: The two-component system (TCS) enables bacteria to sense and respond to environmental changes through histidine kinase-mediated signaling cascades. Although the core components of TCSs have been ...The two-component system (TCS) enables bacteria to sense and respond to environmental changes through histidine kinase-mediated signaling cascades. Although the core components of TCSs have been extensively studied, the molecular basis of accessory proteins in modulating histidine kinase activity remains poorly understood. Here, we report that the outer membrane lipoprotein QseG functions as an accessory protein that directly binds to and activates the histidine kinase QseE via its C-terminal domain. Cryo-electron microscopy (Cryo-EM) structural analysis of the QseG-QseE complex reveals a novel yet conserved interaction mode between an accessory lipoprotein and a histidine kinase, which bridges the outer membrane to cytoplasm. Furthermore, systematic truncation assays and photo-crosslinking experiments indicate that outer membrane-anchored QseG is sufficient and prone to engage with and activate the inner membrane histidine kinase QseE under cultured conditions. Our findings provide mechanistic details for accessory lipoprotein-mediated TCS activation, expanding our understanding of bacterial signaling. The evolutionary conservation of this interaction across bacterial pathogens underscores its broad biological significance and potential as a therapeutic target.IMPORTANCEThe classical TCS system in bacterial signal transduction is composed of two proteins-a histidine kinase and its cognate response regulator. More and more studies have revealed the presence of accessory proteins that can modulate the histidine kinase activity and affect signal transduction, but their mechanisms remain largely elusive. This study unveils a previously unrecognized mechanism by which bacterial accessory lipoproteins mediate TCS activation. We provide compelling evidence that QseG directly interacts with QseE through an evolutionarily conserved structural interface, readily and sufficiently activating QseE's autokinase activity and downstream signaling. Given the essential role of QseEF in bacterial virulence and stress adaptation, our findings pave the way for the development of antimicrobial strategies targeting this conserved lipoprotein-mediated activation mechanism.
History
DepositionFeb 24, 2025Deposition site: PDBJ / Processing site: PDBC
Revision 1.0Nov 19, 2025Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: Quorum-sensing regulator protein G
B: Quorum-sensing regulator protein G
C: histidine kinase
D: histidine kinase


Theoretical massNumber of molelcules
Total (without water)151,5414
Polymers151,5414
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Quorum-sensing regulator protein G / Two-component system QseEF-associated lipoprotein QseG


Mass: 21022.740 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (bacteria)
Gene: yfhG, qseG, SL1344_2525, G1W50_19190, G1W53_19070, G1W54_19660, G1W56_19535, G1W63_19335, G1W64_19365, G1W86_18045, G1W87_18985, G1W89_18830, G1W92_18735, G1X03_18695, G1X04_08460, G1X09_19680, ...Gene: yfhG, qseG, SL1344_2525, G1W50_19190, G1W53_19070, G1W54_19660, G1W56_19535, G1W63_19335, G1W64_19365, G1W86_18045, G1W87_18985, G1W89_18830, G1W92_18735, G1X03_18695, G1X04_08460, G1X09_19680, G1X10_19590, G1X13_19670, G1X17_20470, G1X23_19065, G1X29_19380, G1X32_19630, G1X38_19925, G1X42_18740, G1X47_19355, G1X49_18700, G1X51_19680, G1X52_19370, G1X66_19045, G1X68_16400, G1X69_19950, G1X71_19685, G1X76_19340, G1X80_18180, G1X84_18735, G1X85_19495, G1X86_19670, G1X94_19190, G1X96_19675, G1X99_19370, G1Y02_19370
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A0H3NKH9
#2: Protein histidine kinase


Mass: 54747.652 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (bacteria)
Gene: G1W50_19185, G1W53_19065, G1W54_19655, G1W56_19530, G1W63_19330, G1W64_19360, G1W86_18040, G1W87_18980, G1W89_18825, G1W92_18730, G1X03_18690, G1X04_08455, G1X09_19675, G1X10_19585, G1X13_ ...Gene: G1W50_19185, G1W53_19065, G1W54_19655, G1W56_19530, G1W63_19330, G1W64_19360, G1W86_18040, G1W87_18980, G1W89_18825, G1W92_18730, G1X03_18690, G1X04_08455, G1X09_19675, G1X10_19585, G1X13_19665, G1X17_20465, G1X23_19060, G1X29_19375, G1X32_19625, G1X38_19920, G1X42_18735, G1X47_19350, G1X49_18695, G1X51_19675, G1X52_19365, G1X66_19040, G1X68_16395, G1X69_19945, G1X71_19680, G1X76_19335, G1X80_18175, G1X84_18730, G1X85_19490, G1X86_19665, G1X94_19185, G1X96_19670, G1X99_19365, G1Y02_19365
Production host: Escherichia coli BL21(DE3) (bacteria) / References: UniProt: A0A718UUF8, histidine kinase
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: QseG58-220 and QseE sensor complex / Type: COMPLEX / Entity ID: all / Source: MULTIPLE SOURCES
Source (natural)Organism: Salmonella enterica subsp. enterica serovar Typhimurium str. SL1344 (bacteria)
Source (recombinant)Organism: Escherichia coli BL21(DE3) (bacteria)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 500 nm
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k)

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Processing

EM softwareName: PHENIX / Version: 1.20.1_4487 / Category: model refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 88834 / Symmetry type: POINT
RefinementHighest resolution: 3.9 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)

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