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- EMDB-42602: Campylobacter jejuni CosR apo form -

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Basic information

Entry
Database: EMDB / ID: EMD-42602
TitleCampylobacter jejuni CosR apo form
Map data
Sample
  • Complex: CosR
    • Protein or peptide: DNA-binding response regulator
KeywordsCampylobacter jejuni / CosR / transcriptional regulator / DNA BINDING PROTEIN
Function / homology
Function and homology information


phosphorelay response regulator activity / protein-DNA complex / transcription cis-regulatory region binding / regulation of DNA-templated transcription / cytosol
Similarity search - Function
OmpR/PhoB-type DNA-binding domain / Transcriptional regulatory protein, C terminal / OmpR/PhoB-type DNA-binding domain profile. / Transcriptional regulatory protein, C terminal / Transcriptional regulatory protein WalR-like / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / Winged helix-like DNA-binding domain superfamily
Similarity search - Domain/homology
Homeostatic response regulator transcription factor HsrA
Similarity search - Component
Biological speciesCampylobacter jejuni (Campylobacter)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.77 Å
AuthorsZhang Z
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: mBio / Year: 2024
Title: Structural basis of DNA recognition of the CosR regulator.
Authors: Zhemin Zhang / Yuqi Yan / Jinji Pang / Lei Dai / Qijing Zhang / Edward W Yu /
Abstract: is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, is increasingly ... is a foodborne pathogen commonly found in the intestinal tracts of animals. This pathogen is a leading cause of gastroenteritis in humans. Besides its highly infectious nature, is increasingly resistant to a number of clinically administrated antibiotics. As a consequence, the Centers for Disease Control and Prevention has designated antibiotic-resistant as a serious antibiotic resistance threat in the United States. The CosR regulator is essential to the viability of this bacterium and is responsible for regulating the expression of a number of oxidative stress defense enzymes. Importantly, it also modulates the expression of the CmeABC multidrug efflux system, the most predominant and clinically important system in that mediates resistance to multiple antimicrobials. Here, we report structures of apo-CosR and CosR bound with a 21 bp DNA sequence located at the promotor region using both single-particle cryo-electron microscopy and X-ray crystallography. These structures allow us to propose a novel mechanism for CosR regulation that involves a long-distance conformational coupling and rearrangement of the secondary structural elements of the regulator to bind target DNA.
IMPORTANCE: has emerged as an antibiotic-resistant threat worldwide. CosR is an essential regulator for this bacterium and is important for adaptation to various stresses. Here, we describe the ...IMPORTANCE: has emerged as an antibiotic-resistant threat worldwide. CosR is an essential regulator for this bacterium and is important for adaptation to various stresses. Here, we describe the structural basis of CosR binding to target DNA as determined by cryo-electron microscopy and X-ray crystallography. Since CosR is a potential target for intervention, our studies may facilitate the development of novel therapeutics to combat infection.
History
DepositionNov 2, 2023-
Header (metadata) releaseJan 31, 2024-
Map releaseJan 31, 2024-
UpdateApr 3, 2024-
Current statusApr 3, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_42602.png

Downloads & links

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Map

FileDownload / File: emd_42602.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.67 Å/pix.
x 360 pix.
= 239.76 Å		0.67 Å/pix.
x 360 pix.
= 239.76 Å		0.67 Å/pix.
x 360 pix.
= 239.76 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.666 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.05
Minimum - Maximum-0.11887459 - 0.318448
Average (Standard dev.)-0.00015538231 (±0.004207927)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 239.76001 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_42602_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_42602_half_map_2.map
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Sample components

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Entire : CosR

EntireName: CosR
Components
  • Complex: CosR
    • Protein or peptide: DNA-binding response regulator

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Supramolecule #1: CosR

SupramoleculeName: CosR / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Campylobacter jejuni (Campylobacter)

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Macromolecule #1: DNA-binding response regulator

MacromoleculeName: DNA-binding response regulator / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Campylobacter jejuni (Campylobacter)
Molecular weightTheoretical: 25.56127 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MGRILVIEDE ISLNKTIIDN LNEFGYQTDS SENFKDGEYF IGIRHYDLVL ASWNLPDGDG AELVNTIKHK SPRTSVMIMS AKADKDTEI KALKAGADDF VKKPLDFDIL LARIEARLRL GGTNVIKIED LVIDPDEEKI TYKGQDIELK GKPFEVLTHL A RHSDQIVS ...String:
MGRILVIEDE ISLNKTIIDN LNEFGYQTDS SENFKDGEYF IGIRHYDLVL ASWNLPDGDG AELVNTIKHK SPRTSVMIMS AKADKDTEI KALKAGADDF VKKPLDFDIL LARIEARLRL GGTNVIKIED LVIDPDEEKI TYKGQDIELK GKPFEVLTHL A RHSDQIVS KEQLLDAIWE EPELVTPNVI EVAINQIRQK MDKPLNISTI ETVRRRGYRF CFPKKS

UniProtKB: Homeostatic response regulator transcription factor HsrA

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 54.6 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.8 µm / Nominal magnification: 165000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 1504675
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.77 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 31260
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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