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- EMDB-71309: Structure of P. gingivalis PorK and PorN complexes from cryo elec... -

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Basic information

Entry
Database: EMDB / ID: EMD-71309
TitleStructure of P. gingivalis PorK and PorN complexes from cryo electron microscopy
Map data
Sample
  • Complex: PorK/N protein complex
    • Protein or peptide: Gliding motility protein GldN
    • Protein or peptide: Lipoprotein, putative
  • Ligand: beta-D-mannopyranose
  • Ligand: CALCIUM ION
KeywordsT9SS / porphyromonas gingivalis / TRANSPORT PROTEIN
Function / homology
Function and homology information


formylglycine-generating oxidase activity
Similarity search - Function
Gliding motility associated protein GldN / Gliding motility associated protein GldN / : / Sulfatase-modifying factor enzyme / Sulfatase-modifying factor enzyme 1-like domain / Sulfatase-modifying factor enzyme superfamily / C-type lectin fold / Prokaryotic membrane lipoprotein lipid attachment site profile.
Similarity search - Domain/homology
Gliding motility protein GldN / Lipoprotein, putative
Similarity search - Component
Biological speciesPorphyromonas gingivalis (bacteria) / Porphyromonas gingivalis W83 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.75 Å
AuthorsHanssen E / Morton C / Gorasia DG / Veith PD / Reynolds EC
Funding support Australia, 2 items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)1123866 Australia
National Health and Medical Research Council (NHMRC, Australia)1193647 Australia
Citation
Journal: Nat Commun / Year: 2025
Title: Insights into type IX secretion from PorKN cogwheel structure bound to PorG and attachment complexes.
Authors: Dhana G Gorasia / Eric Hanssen / Manasi Mudaliyar / Craig J Morton / Sepideh Valimehr / Christine Seers / Lianyi Zhang / Matthew T Doyle / Debnath Ghosal / Paul D Veith / Eric C Reynolds /
Abstract: The Type IX Secretion System exports proteins across the outer membrane (OM) of bacteria in the Bacteroidota phylum, however, the mechanistic details remain unknown. In Porphyromonas gingivalis the ...The Type IX Secretion System exports proteins across the outer membrane (OM) of bacteria in the Bacteroidota phylum, however, the mechanistic details remain unknown. In Porphyromonas gingivalis the core components of the multi-protein complex are the Sov translocon, Attachment Complexes (PorQ, U, V, Z), PorLM molecular motors and PorKN rings. Here, we present a ~ 3.5 Å cryo-EM structure of the periplasmic rings comprising 32-33 subunits each of PorK and PorN. Additionally, we show the presence of a critical disulfide bond between PorK and the OM protein PorG that is essential for protein secretion and demonstrate that the Attachment Complexes bind to, and are localized above, the PorKN rings. Overall, each ring resembles a cogwheel with PorN forming cog-like projections that we propose engage with the PorLM motor to drive the rotation of the PorKN cogwheel together with PorG and associated Attachment Complexes, thus providing the energy to complete protein secretion and the coordinated cell surface attachment of the secreted cargo.
#1: Journal: Biorxiv / Year: 2025
Title: Near-atomic structure of the PorKN rings, disulfide bonded to PorG and bound to Attachment Complexes, provide mechanistic insights into the type IX secretion system
Authors: Gorasia D / Hanssen E / Mudaliyar M / Morton C / Valimehr S / Seers C / Zhang L / Ghosal D / Veith P / Reynolds E
History
DepositionJun 19, 2025-
Header (metadata) releaseJul 16, 2025-
Map releaseJul 16, 2025-
UpdateSep 3, 2025-
Current statusSep 3, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_71309.png

Downloads & links

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Map

FileDownload / File: emd_71309.map.gz / Format: CCP4 / Size: 30.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.32 Å/pix.
x 200 pix.
= 264. Å		1.32 Å/pix.
x 200 pix.
= 264. Å		1.32 Å/pix.
x 200 pix.
= 264. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.32 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.12
Minimum - Maximum-0.49457595 - 1.1346011
Average (Standard dev.)0.0049728784 (±0.03633248)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions200200200
Spacing200200200
CellA=B=C: 264.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_71309_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_71309_half_map_1.map
Projections & Slices
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Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_71309_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : PorK/N protein complex

EntireName: PorK/N protein complex
Components
  • Complex: PorK/N protein complex
    • Protein or peptide: Gliding motility protein GldN
    • Protein or peptide: Lipoprotein, putative
  • Ligand: beta-D-mannopyranose
  • Ligand: CALCIUM ION

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Supramolecule #1: PorK/N protein complex

SupramoleculeName: PorK/N protein complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Porphyromonas gingivalis (bacteria) / Strain: W83
Molecular weightTheoretical: 3.5 MDa

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Macromolecule #1: Gliding motility protein GldN

MacromoleculeName: Gliding motility protein GldN / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Porphyromonas gingivalis W83 (bacteria) / Strain: W83
Molecular weightTheoretical: 30.080869 KDa
SequenceString: LSNRAQEFNR RLTQKTDNAP WRRVVYRRVD LMEESNAVLY YPPRPIGDRK NLFSTIFGLI NSNSLDVYEY LDGFEAFTDQ YKIKFQEFL DRFGIYYQPS TNKNAELFKV ADSDIPSAEV KAYYVKEEWY FTPTNSDVDI KIQAICPIMT GQDEFGEVRN Q PLFWIPYE ...String:
LSNRAQEFNR RLTQKTDNAP WRRVVYRRVD LMEESNAVLY YPPRPIGDRK NLFSTIFGLI NSNSLDVYEY LDGFEAFTDQ YKIKFQEFL DRFGIYYQPS TNKNAELFKV ADSDIPSAEV KAYYVKEEWY FTPTNSDVDI KIQAICPIMT GQDEFGEVRN Q PLFWIPYE NIRPYIARER VMLSSLNNTR NSTIDDFFRL NLYKGDIVKT ENLHNRALAE YCPTPDSMKM ESKRIDKELQ GF RDGLFVT QDTTWMK

UniProtKB: Gliding motility protein GldN

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Macromolecule #2: Lipoprotein, putative

MacromoleculeName: Lipoprotein, putative / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Porphyromonas gingivalis W83 (bacteria) / Strain: W83
Molecular weightTheoretical: 51.184895 KDa
SequenceString: ELTGAKLSSW NEPSPFGMIQ VPRGSIVLGN KEADSLWGIP AESRPISVDA FWMDRTEITN AQYRQFVYYV RDSIIRERLA DPAYGGNEE YKITENKFGE PVTPHLDWSK PIPSEKRATE EEIAAINSVY YTNPVTHDRK LNPDQMVYRY EVYDYRSAAL R EHQLKAAK ...String:
ELTGAKLSSW NEPSPFGMIQ VPRGSIVLGN KEADSLWGIP AESRPISVDA FWMDRTEITN AQYRQFVYYV RDSIIRERLA DPAYGGNEE YKITENKFGE PVTPHLDWSK PIPSEKRATE EEIAAINSVY YTNPVTHDRK LNPDQMVYRY EVYDYRSAAL R EHQLKAAK RNLNTDIKVD PNAVVMISKD TAFVDESGNI ISETITRPLS SEYDFLNTYI VPIYPDETCW VNDFPNARTE IY TRMYFNH PGYDDYPVVG ISWEQAQAFC AWRSEFFRKG IRLPEGQIMD DFRLPTEAEW EYAARMGDSN NKYPWSTEDL RTG RGCFLG NFKPGEGDYT ADGHLIPSRV SSFSPNDFGL YDMAGNVAEW TSTAFSESGL KQMSDINPEL EYKAALTDPY ILKQ KVVRG GSWKDVARFI RSATRSHEYQ NVGRSYIGFR CVRTSIAFSS GK

UniProtKB: Lipoprotein, putative

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Macromolecule #5: beta-D-mannopyranose

MacromoleculeName: beta-D-mannopyranose / type: ligand / ID: 5 / Number of copies: 2 / Formula: BMA
Molecular weightTheoretical: 180.156 Da
Chemical component information

ChemComp-BMA:
beta-D-mannopyranose

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Macromolecule #6: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 6 / Number of copies: 1 / Formula: CA
Molecular weightTheoretical: 40.078 Da

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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

Concentration1.2 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
50.0 mMC4H11NO3.HClTris-HCL
50.0 mMNaClSodium chloride
0.5 %C24H46O11n-Dodecyl-B-D-maltoside
1.0 MCH4N2OUrea
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY ARRAY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR / Details: 15mA
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 295 K / Instrument: FEI VITROBOT MARK IV / Details: Blot forace -1 blot time 3sec sample size 4ul.

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 10 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 1 / Number real images: 8909 / Average exposure time: 5.34 sec. / Average electron dose: 54.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.6 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 64000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 556522
CTF correctionSoftware - Name: cryoSPARC (ver. 4.5.1) / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.75 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.5.1) / Number images used: 69982
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5.1)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

9myj


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9p6h:
Structure of P. gingivalis PorK and PorN complexes from cryo electron microscopy

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