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- PDB-9mvv: Pfs230 (D9-D14) with Pfs48/45 of the endogenous Pfs230-Pfs48/45 c... -

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Basic information

Entry
Database: PDB / ID: 9mvv
TitlePfs230 (D9-D14) with Pfs48/45 of the endogenous Pfs230-Pfs48/45 complex
Components
  • Gametocyte surface protein P230
  • Gametocyte surface protein P45/48
KeywordsPROTEIN BINDING / 6-cysteine protein / Plasmodium falciparum / malaria transmission
Function / homology
Function and homology information


side of membrane / cell surface / plasma membrane
Similarity search - Function
: / 6-Cysteine (6-Cys) domain / 6-Cysteine (6-Cys) domain superfamily / Sexual stage antigen s48/45 domain / 6-Cysteine (6-Cys) domain profile. / Sexual stage antigen s48/45 domain
Similarity search - Domain/homology
Gametocyte surface protein P230 / Gametocyte surface protein P45/48
Similarity search - Component
Biological speciesPlasmodium falciparum (malaria parasite P. falciparum)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.36 Å
AuthorsDietrich, M.H. / Glukhova, A. / Shakeel, S. / Tham, W.H.
Funding support Australia, 2items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP2001385 Australia
National Health and Medical Research Council (NHMRC, Australia)APP2016908 Australia
CitationJournal: Science / Year: 2025
Title: Cryo-EM structure of endogenous Pfs230 and Pfs48/45 fertilization complex.
Authors: Melanie H Dietrich / Jill Chmielewski / Li-Jin Chan / Li Lynn Tan / Amy Adair / Frankie M T Lyons / Mikha Gabriela / Sash Lopaticki / Toby A Dite / Laura F Dagley / Lucia Pazzagli / Priya ...Authors: Melanie H Dietrich / Jill Chmielewski / Li-Jin Chan / Li Lynn Tan / Amy Adair / Frankie M T Lyons / Mikha Gabriela / Sash Lopaticki / Toby A Dite / Laura F Dagley / Lucia Pazzagli / Priya Gupta / Mohd Kamil / Ashley M Vaughan / Rattanaporn Rojrung / Anju Abraham / Ramin Mazhari / Rhea J Longley / Kathleen Zeglinski / Quentin Gouil / Ivo Mueller / Stewart A Fabb / Rekha Shandre-Mugan / Colin W Pouton / Alisa Glukhova / Shabih Shakeel / Wai-Hong Tham /
Abstract: Malaria parasite fertilization occurs in the midgut of a female mosquito. Blocking fertilization within the mosquito can prevent malaria transmission. Pfs230 and Pfs48/45 proteins are critical for ...Malaria parasite fertilization occurs in the midgut of a female mosquito. Blocking fertilization within the mosquito can prevent malaria transmission. Pfs230 and Pfs48/45 proteins are critical for male fertility and transmission of the malaria parasite. They form a core fertilization complex, but it is unknown how they interact. We determined a cryo-electron microscopy structure of the endogenous Pfs230-Pfs48/45 complex showing that Pfs48/45 interacts with Pfs230 domains 13 and 14. Transgenic parasite lines with these domains removed were defective in Pfs230 gamete localization and showed reduced oocyst formation. Nanobodies against domains 13 and 14 inhibited Pfs230-Pfs48/45 complex formation and reduced transmission, and structural analyses revealed their epitopes. These Pfs230 domains were targets of naturally acquired immunity and immune sera from messenger RNA lipid nanoparticle immunizations blocked parasite transmission.
History
DepositionJan 16, 2025Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 30, 2025Provider: repository / Type: Initial release
Revision 1.0Jul 30, 2025Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jul 30, 2025Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jul 30, 2025Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release
Revision 1.1Aug 13, 2025Group: Data collection / Database references / Category: citation / citation_author / em_admin
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _em_admin.last_update
Revision 1.2Sep 24, 2025Group: Data collection / Database references / Category: citation / em_admin / Item: _citation.journal_volume / _em_admin.last_update

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Gametocyte surface protein P230
C: Gametocyte surface protein P45/48


Theoretical massNumber of molelcules
Total (without water)412,2082
Polymers412,2082
Non-polymers00
Water00
1


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

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Components

#1: Protein Gametocyte surface protein P230


Mass: 363701.750 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Plasmodium falciparum (malaria parasite P. falciparum)
References: UniProt: P68874
#2: Protein Gametocyte surface protein P45/48


Mass: 48506.062 Da / Num. of mol.: 1 / Source method: isolated from a natural source
Source: (natural) Plasmodium falciparum (malaria parasite P. falciparum)
References: UniProt: Q8I6T1
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: Heterodimeric complex of endogenous Plasmodium falciparum proteins Pfs230 and Pfs48/45
Type: COMPLEX / Entity ID: all / Source: NATURAL
Molecular weightValue: 0.4 MDa / Experimental value: NO
Source (natural)Organism: Plasmodium falciparum (malaria parasite P. falciparum)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: GOLD / Grid type: UltrAuFoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 %

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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: 1600 nm / Nominal defocus min: 400 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm
Specimen holderCryogen: NITROGEN
Image recordingElectron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameCategory
1cryoSPARCparticle selection
4cryoSPARCCTF correction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.36 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 87061 / Symmetry type: POINT
RefinementCross valid method: NONE
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
Displacement parametersBiso mean: 104.34 Å2
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.003510668
ELECTRON MICROSCOPYf_angle_d0.754114529
ELECTRON MICROSCOPYf_chiral_restr0.05561707
ELECTRON MICROSCOPYf_plane_restr0.00581855
ELECTRON MICROSCOPYf_dihedral_angle_d5.65611459

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