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- EMDB-16415: HB3VAR03 apo headstructure (PfEMP1 A) -

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Basic information

Entry
Database: EMDB / ID: EMD-16415
TitleHB3VAR03 apo headstructure (PfEMP1 A)
Map data
Sample
  • Complex: Multidomain architecture of PfEMP1 A
    • Protein or peptide: PfEMP1
KeywordsPlasmodium falciparum / Cerebral Malaria / PfEMP1 / EPCR / Cell adhesion
Function / homology
Function and homology information


host cell surface receptor binding / membrane
Similarity search - Function
: / PfEMP1 protein, CIDRalpha1 domain / Plasmodium falciparum erythrocyte membrane protein-1, N-terminal segment / N-terminal segments of PfEMP1 / Cysteine-rich interdomain region 1 gamma / Cysteine-Rich Interdomain Region 1 gamma / Duffy-binding-like domain, C-terminal subdomain / Duffy-binding-like domain / PFEMP1 DBL domain / Duffy-antigen binding ...: / PfEMP1 protein, CIDRalpha1 domain / Plasmodium falciparum erythrocyte membrane protein-1, N-terminal segment / N-terminal segments of PfEMP1 / Cysteine-rich interdomain region 1 gamma / Cysteine-Rich Interdomain Region 1 gamma / Duffy-binding-like domain, C-terminal subdomain / Duffy-binding-like domain / PFEMP1 DBL domain / Duffy-antigen binding / Duffy-antigen binding superfamily / Duffy binding domain
Similarity search - Domain/homology
Biological speciesPlasmodium falciparum HB3 (eukaryote)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsRaghavan SSR / Lavstsen T / Wang KT
Funding support Denmark, 2 items
OrganizationGrant numberCountry
Danish Council for Independent Research9039-00285A Denmark
LundbeckfondenR344-2020-934 Denmark
CitationJournal: Structure / Year: 2023
Title: Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1.
Authors: Sai Sundar Rajan Raghavan / Louise Turner / Rasmus W Jensen / Nicolai Tidemand Johansen / Daniel Skjold Jensen / Pontus Gourdon / Jinqiu Zhang / Yong Wang / Thor Grundtvig Theander / Kaituo ...Authors: Sai Sundar Rajan Raghavan / Louise Turner / Rasmus W Jensen / Nicolai Tidemand Johansen / Daniel Skjold Jensen / Pontus Gourdon / Jinqiu Zhang / Yong Wang / Thor Grundtvig Theander / Kaituo Wang / Thomas Lavstsen /
Abstract: Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum ...Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRα1 domains interact with the adjacent DBLα1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLα1 domain is displaced, and the EPCR-binding helix of CIDRα1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family.
History
DepositionDec 29, 2022-
Header (metadata) releaseAug 2, 2023-
Map releaseAug 2, 2023-
UpdateOct 9, 2024-
Current statusOct 9, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_16415.png

Downloads & links

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Map

FileDownload / File: emd_16415.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 300 pix.
= 249.6 Å		0.83 Å/pix.
x 300 pix.
= 249.6 Å		0.83 Å/pix.
x 300 pix.
= 249.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.832 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.3
Minimum - Maximum-1.0932204 - 2.2085094
Average (Standard dev.)0.000094038056 (±0.05068671)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 249.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_16415_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_16415_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 : Multidomain architecture of PfEMP1 A

EntireName: Multidomain architecture of PfEMP1 A
Components
  • Complex: Multidomain architecture of PfEMP1 A
    • Protein or peptide: PfEMP1

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Supramolecule #1: Multidomain architecture of PfEMP1 A

SupramoleculeName: Multidomain architecture of PfEMP1 A / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Plasmodium falciparum HB3 (eukaryote)
Molecular weightTheoretical: 145 KDa

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Macromolecule #1: PfEMP1

MacromoleculeName: PfEMP1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Plasmodium falciparum HB3 (eukaryote)
Molecular weightTheoretical: 145.128734 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MASSASKFSK IVVGNETHKS ARNVLEGFAK DIKGKASIDA EKHAYSLKGN LKDAKFNHDF FKIKSDMPGN PCYLDFAFHS NTPGNQREY RHPCARSMNK NLFNLEGAVC TNSKIKGNEE KINGAGACAP YRRRHICDLN LEHIDVHNVQ NIHDLLGNVL V TAKYEGES ...String:
MASSASKFSK IVVGNETHKS ARNVLEGFAK DIKGKASIDA EKHAYSLKGN LKDAKFNHDF FKIKSDMPGN PCYLDFAFHS NTPGNQREY RHPCARSMNK NLFNLEGAVC TNSKIKGNEE KINGAGACAP YRRRHICDLN LEHIDVHNVQ NIHDLLGNVL V TAKYEGES IVEKHPNRGS SEVCTALARS FADIGDIIRG KDLYLGHEQG NNKLEARLKT IFQNIKNKNK SPLDKLSLEQ VR EYWWALN REDVWKALTC FADGSEEYFI QSSDKEHSFS SEYCGHEQGN VPTNLDYVPQ FLRWFDEWAD DFCRIKKIKL ENV KNACRD EKKRKYCSLN GFDCTQTIWK KGVLHRSNEC TGCLVKCNPY EIWLGNQREA FRKQKEKYEN EIKTYVHDTG ISNS NINNE YYKEFYKILK NNNYETANEF IKLLNEGRYC NKKEKIEEEE DIDFTNTNEK GTFYRSDYCQ VCPDCGVECK NETCT PKTV IYPDCGKNEK YEPPGDAKNT EINVINSGDK EGYIFEKLSE FCTNENNENG KNYEQWKCYY DNKKNNNKCK MEINIA NSK LKNKITSFDE FFDFWVRKLL IDTIKWETEL TYCINNTDVT DCNKCNKNCV CFDKWVKQKE DEWTNIMKLF TNKHDIP KK YYLNINDLFD SFFFQVIYKF NEGEAKWNEL KENLKKQIAS SKANNGTKDS EAAIKVLFNH IKEIATICKD NNTNEGCD P SVDSKTNSCG KNTKAGSDKV ISVKQIAQYY KRIAHKQLNE RGSRSALKGD ASKGTYKKNG TPSNLKEICE ITAKHSNDS RRDGEPCTGK DGGQVRVRTK IGTPWTKIVE INKTSYKEVF LPPRRQHMCT SNLEHLNTGN KGLKDGKLAI HSLLGDVLLA AKEQANFIK NKYKRQKASN GFKDKGTICR AIRYSYADLG DIIKGTDLWE ANPGEKNTQR RLKTVFGIIK KNMPGIKDNQ K YKDDEKNN PPYKLLREDW WEANRDQVWQ AMKCAMKNGI TCGSSDHTPL DDYIPQKLRW LTEWAEWYCK AQSKEYEKLK EK CKECKGN DQCTQDTPDC EKCKAACKKY GKNIKTWEDQ WKVISSKYKE LYKQAEIYAG NGGPGYYNTK VQEEDKPVVD FLY NLYLQN GGKKGPPPDT HPSKSVTAPL KQVATVDTPS TVYSTPEGYI HQEAAMDCKQ QHVFCDDNSG GKDDNKQYAF RHQP HDYDE ALRCDQRDKP PPESKKVEKA KKEKDENDDG GSHHHHHHGG GSAHIVMVDA YKPTK

UniProtKB: PfEMP1

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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

Concentration0.5 mg/mL
BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 48.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 750035
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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