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- EMDB-17587: Single particle cryo-EM of the P140-P110 heterodimer of Mycoplasm... -

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Basic information

Entry
Database: EMDB / ID: EMD-17587
TitleSingle particle cryo-EM of the P140-P110 heterodimer of Mycoplasma genitalium at 3.3 Angstrom resolution.
Map data
Sample
  • Complex: P140-P110 Heterodimer
    • Complex: Mgp-operon protein 3
      • Protein or peptide: Mgp-operon protein 3
    • Complex: Adhesin P1
      • Protein or peptide: Adhesin P1
KeywordsAdhesion / Mycoplasma genitalium / CELL ADHESION
Function / homology
Function and homology information


adhesion of symbiont to microvasculature / cell adhesion / plasma membrane
Similarity search - Function
Adhesin P1, C-terminal domain / Adhesin P1, N-terminal / Adhesin P1 / Mycoplasma adhesin P1, C-terminal / Mycoplasma adhesin P1, N-terminal / MgpC adhesin / Mgp-operon protein 3, C-terminal domain / MgpC adhesin / MGP3 C-terminal domain
Similarity search - Domain/homology
Adhesin P1 / Mgp-operon protein 3
Similarity search - Component
Biological speciesMycoplasmoides genitalium G37 (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsSprankel L / Scheffer MP / Frangakis AS
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)FR 1653/6-3 Germany
German Research Foundation (DFG)GRK 2566/1 Germany
CitationJournal: PLoS Pathog / Year: 2023
Title: Cryo-electron tomography reveals the binding and release states of the major adhesion complex from Mycoplasma genitalium.
Authors: Lasse Sprankel / Margot P Scheffer / Sina Manger / Utz H Ermel / Achilleas S Frangakis /
Abstract: The nap particle is an immunogenic surface adhesion complex from Mycoplasma genitalium. It is essential for motility and responsible for binding sialylated oligosaccharides on the surface of the host ...The nap particle is an immunogenic surface adhesion complex from Mycoplasma genitalium. It is essential for motility and responsible for binding sialylated oligosaccharides on the surface of the host cell. The nap particle is composed of two P140-P110 heterodimers, the structure of which was recently solved. However, the interpretation of the mechanism by which the mycoplasma cells orchestrate adhesion remained challenging. Here, we provide cryo-electron tomography structures at ~11 Å resolution, which allow for the distinction between the bound and released state of the nap particle, displaying the in vivo conformational states. Fitting of the atomically resolved structures reveals that bound sialylated oligosaccharides are stabilized by both P110 and P140. Movement of the stalk domains allows for the transfer of conformational changes from the interior of the cell to the binding pocket, thus having the capability of an active release process. It is likely that the same mechanism can be transferred to other Mycoplasma species that belong to the pneumoniae cluster.
History
DepositionJun 9, 2023-
Header (metadata) releaseNov 1, 2023-
Map releaseNov 1, 2023-
UpdateNov 22, 2023-
Current statusNov 22, 2023Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_17587.png

Downloads & links

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Map

FileDownload / File: emd_17587.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.05 Å
Density
Contour LevelBy AUTHOR: 0.4
Minimum - Maximum-1.6638378 - 2.599626
Average (Standard dev.)0.0014922218 (±0.07673825)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 315.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_17587_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_17587_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_17587_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : P140-P110 Heterodimer

EntireName: P140-P110 Heterodimer
Components
  • Complex: P140-P110 Heterodimer
    • Complex: Mgp-operon protein 3
      • Protein or peptide: Mgp-operon protein 3
    • Complex: Adhesin P1
      • Protein or peptide: Adhesin P1

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Supramolecule #1: P140-P110 Heterodimer

SupramoleculeName: P140-P110 Heterodimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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Supramolecule #2: Mgp-operon protein 3

SupramoleculeName: Mgp-operon protein 3 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Mycoplasmoides genitalium G37 (bacteria)

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Supramolecule #3: Adhesin P1

SupramoleculeName: Adhesin P1 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Mycoplasmoides genitalium G37 (bacteria)

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Macromolecule #1: Mgp-operon protein 3

MacromoleculeName: Mgp-operon protein 3 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycoplasmoides genitalium G37 (bacteria)
Molecular weightTheoretical: 115.382062 KDa
Recombinant expressionOrganism: Mycoplasmoides genitalium G37 (bacteria)
SequenceString: MKTMRKQIYK KAYWLLLPFL PLALANTFLV KEDSKNVTAY TPFATPITDS KSDLVSLAQL DSSYQIADQT IHNTNLFVLF KSRDVKVKY ESSGSNNISF DSTSQGEKPS YVVEFTNSTN IGIKWTMVKK YQLDVPNVSS DMNQVLKNLI LEQPLTKYTL N SSLAKEKG ...String:
MKTMRKQIYK KAYWLLLPFL PLALANTFLV KEDSKNVTAY TPFATPITDS KSDLVSLAQL DSSYQIADQT IHNTNLFVLF KSRDVKVKY ESSGSNNISF DSTSQGEKPS YVVEFTNSTN IGIKWTMVKK YQLDVPNVSS DMNQVLKNLI LEQPLTKYTL N SSLAKEKG KTQREVHLGS GQANQWTSQR NQHDLNNNPS PNASTGFKLT TGNAYRKLSE SWPIYEPIDG TKQGKGKDSS GW SSTEENE AKNDAPSVSG GGSSSGTFNK YLNTKQALES IGILFDDQTP RNVITQLYYA STSKLAVTNN HIVVMGNSFL PSM WYWVVE RSAQENASNK PTWFANTNLD WGEDKQKQFV ENQLGYKETT STNSHNFHSK SFTQPAYLIS GIDSVNDQII FSGF KAGSV GYDSSSSSSS SSSSSTKDQA LAWSTTTSLD SKTGYKDLVT NDTGLNGPIN GSFSIQDTFS FVVPYSGNHT NNGTT GPIK TAYPVKKDQK STVKINSLIN ATPLNSYGDE GIGVFDALGL NYNFKSNQER LPSRTDQIFV YGIVSPNELR SAKSSA DST GSDTKVNWSN TQSRYLPVPY NYSEGIIDAD GFKRPENRGA SVTTFSGLKS IAPDGFANSI ANFSVGLKAG IDPNPVM SG KKANYGAVVL TRGGVVRLNF NPGNDSLLST TDNNIAPISF SFTPFTAAES AVDLTTFKEV TYNQESGLWS YIFDSSLK P SHDGKQTPVT DNMGFSVITV SRTGIELNQD QATTTLDVAP SALAVQSGIQ STTQTLTGVL PLSEEFSAVI AKDSDQNKI DIYKNNNGLF EIDTQLSNSV ATNNGGLAPS YTENRVDAWG KVEFADNSVL QARNLVDKTV DEIINTPEIL NSFFRFTPAF EDQKATLVA TKQSDTSLSV SPRIQFLDGN FYDLNSTIAG VPLNIGFPSR VFAGFAALPA WVIPVSVGSS VGILFILLVL G LGIGIPMY RVRKLQDASF VNVFKKVDTL TTAVGSVYKK IITQTGVVKK APSALKAANP SVKKPAAFLK PPVQPPSKPE GE QKAVEVK SEETKSHHHH HH

UniProtKB: Mgp-operon protein 3

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Macromolecule #2: Adhesin P1

MacromoleculeName: Adhesin P1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Mycoplasmoides genitalium G37 (bacteria)
Molecular weightTheoretical: 159.809297 KDa
SequenceString: MHQPKKRLAK KSWAFLTAAL TLGVITGVGG YFLFNQNKQR SSVSNFAYQP KQLSVKHQQA VDETLTPWTW NNNNFSSLKI TGENPGSFG LVRSQNDNLN ISSVTKNSSD DNLKYLNAVE KYLDGQQNFA IRRYDNNGRA LYDINLAKME NPSTVQRGLN G EPIFDPFK ...String:
MHQPKKRLAK KSWAFLTAAL TLGVITGVGG YFLFNQNKQR SSVSNFAYQP KQLSVKHQQA VDETLTPWTW NNNNFSSLKI TGENPGSFG LVRSQNDNLN ISSVTKNSSD DNLKYLNAVE KYLDGQQNFA IRRYDNNGRA LYDINLAKME NPSTVQRGLN G EPIFDPFK GFGLTGNAPT DWNEIKGKVP VEVVQSPHSP NLYFVLLVPK VALEYHNLNN QVVKESLEVK ATQSSFNPTQ RL QKDSPVK DSSKQGEKLS ETTASSMSSG MATSTRAKAL KVEVERGSQS DSLLKNDFAK KPLKHKNSSG EVKLEAEKEF TEA WKPLLT TDQIAREKGM GATVVSFYDA PYSENHTAFG LVDHIDPKKM VENYPPSWKT PKWNHHGIWD YNARNLLLQT TGFF NPRRH PEWFDEGQAK ADNTSPGFKV GDTDHKKDGF KKNSSSPIAL PFEAYFANIG NMVAIGNSVF IFGGNGHATK MFTTN PLSI GVFRIKYTDN FSKSSVTGWP YAVLFGGLIN PQTNGLKDLP LGTNRWFEYV PRMAVSGVKW VGNQLVLAGT LTMGDT ATV PRLKYDQLEK HLNLVAQGQG LLREDLQIFT PYGWANRPDI PVGAWLQDEM GSKFGPHYFL NNPDIQDNVN NDTVEAL IS SYKNTDKLKH VYPYRYSGLY AWQLFNWSNK LTNTPLSANF VNENSYAPNS LFAAILNEDL LTGLSDKIFY GKENEFAE N EADRFNQLLS LNPNPNTNWA RYLNVVQRFT TGPNLDSSTF DQFLDFLPWI GNGKPFSNSP SPSTSASSST PLPTFSNIN VGVKSMITQH LNKENTRWVF IPNFSPDIWT GAGYRVQSAN QKNGIPFEQV KPSNNSTPFD PNSDDNKVTP SGGSSKPTTY PALPNSISP TSDWINALTF TNKNNPQRNQ LLLRSLLGTI PVLINKSGDS NDQFNKDSEQ KWDKTETNEG NLPGFGEVNG L YNAALLHT YGFFGTNTNS TDPKIGFKAD SSSSSSSTLV GSGLNWTSQD VGNLVVINDT SFGFQLGGWF ITFTDFIRPR TG YLGITLS SLQDQTIIWA DQPWTSFKGS YLDSDGTPKS LWDPTALKSL PNSSTTYDTN PTLSPSFQLY QPNKVKAYQT TNT YNKLIE PVDATSAATN MTSLLKLLTT KNIKAKLGKG TASSQGNNNG GGVSQTINTI TTTGNISEGL KEETSIQAET LKKF FDSKQ NNKSEIGIGD STFTKMDGKL TGVVSTPLVN LINGQGATSD SDTEKISFKP GNQIDFNRLF TLPVTELFDP NTMFV YDQY VPLLVNLPSG FDQASIRLKV ISYSVENQTL GVRLEFKDPQ TQQFIPVLNA SSTGPQTVFQ PFNQWADYVL PLIVTV PIV VIILSVTLGL TIGIPMHRNK KALQAGFDLS NKKVDVLTKA VGSVFKEIIN RTGISNAPKK LKQATPTKPT PKTPPKP PV KQ

UniProtKB: Adhesin P1

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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

Concentration0.025 mg/mL
BufferpH: 7.4
Component:
ConcentrationNameFormula
75.0 mMTris
400.0 mMsodium chlorideNaClSodium chloride
5.0 %Glycerol
0.5 %octylglucoside detergent
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 30 sec. / Pretreatment - Atmosphere: AIR
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Calibrated defocus max: 4.0 µm / Calibrated defocus min: 1.0 µm / Calibrated magnification: 130000 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 4.0 µm / Nominal defocus min: 1.0 µm / Nominal magnification: 130000
Specialist opticsEnergy filter - Name: GIF Quantum SE / Energy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Average electron dose: 50.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 3.3.2)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.3.2) / Number images used: 149542
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

6rut

source_name: PDB, initial_model_type: experimental model

6r3t

chain_id: A, residue_range: 818-936, source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL
Output model

PDB-8pbx:
Single particle cryo-EM of the P140-P110 heterodimer of Mycoplasma genitalium at 3.3 Angstrom resolution.

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