+
Open data
-
Basic information
Entry | Database: EMDB / ID: EMD-10590 | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | Structure of PfMyoA decorated Plasmodium Act1 filament | |||||||||
![]() | Global B-factor sharpening | |||||||||
![]() |
| |||||||||
Function / homology | ![]() plastid inheritance / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | helical reconstruction / ![]() | |||||||||
![]() | Vahokoski J / Calder LJ / Lopez AJ / Rosenthal PB / Kursula I | |||||||||
Funding support | ![]() ![]()
| |||||||||
![]() | ![]() Title: High-resolution structures of malaria parasite actomyosin and actin filaments. Authors: Juha Vahokoski / Lesley J Calder / Andrea J Lopez / Justin E Molloy / Inari Kursula / Peter B Rosenthal / ![]() ![]() ![]() Abstract: Malaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon ...Malaria is responsible for half a million deaths annually and poses a huge economic burden on the developing world. The mosquito-borne parasites (Plasmodium spp.) that cause the disease depend upon an unconventional actomyosin motor for both gliding motility and host cell invasion. The motor system, often referred to as the glideosome complex, remains to be understood in molecular terms and is an attractive target for new drugs that might block the infection pathway. Here, we present the high-resolution structure of the actomyosin motor complex from Plasmodium falciparum. The complex includes the malaria parasite actin filament (PfAct1) complexed with the class XIV myosin motor (PfMyoA) and its two associated light-chains. The high-resolution core structure reveals the PfAct1:PfMyoA interface in atomic detail, while at lower-resolution, we visualize the PfMyoA light-chain binding region, including the essential light chain (PfELC) and the myosin tail interacting protein (PfMTIP). Finally, we report a bare PfAct1 filament structure at improved resolution. | |||||||||
History |
|
-
Structure visualization
Movie |
![]() |
---|---|
Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
-
Downloads & links
-EMDB archive
Map data | ![]() | 44.3 MB | ![]() | |
---|---|---|---|---|
Header (meta data) | ![]() ![]() | 19.9 KB 19.9 KB | Display Display | ![]() |
Images | ![]() | 208.6 KB | ||
Masks | ![]() | 512 MB | ![]() | |
Others | ![]() ![]() ![]() | 408 MB 409.3 MB 409.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6tu7MC ![]() 6tu4C M: atomic model generated by this map C: citing same article ( |
---|---|
Similar structure data |
-
Links
EMDB pages | ![]() ![]() |
---|---|
Related items in Molecule of the Month |
-
Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Annotation | Global B-factor sharpening | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
|
-Supplemental data
-Mask #1
File | ![]() | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Additional map: #1
File | emd_10590_additional_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #2
File | emd_10590_half_map_1.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-Half map: #1
File | emd_10590_half_map_2.map | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Projections & Slices |
| ||||||||||||
Density Histograms |
-
Sample components
-Entire : PfMyoA decorated PfAct1 filament
Entire | Name: PfMyoA decorated PfAct1 filament |
---|---|
Components |
|
-Supramolecule #1: PfMyoA decorated PfAct1 filament
Supramolecule | Name: PfMyoA decorated PfAct1 filament / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2 |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Recombinant expression | Organism: ![]() ![]() ![]() |
-Macromolecule #1: Myosin-A
Macromolecule | Name: Myosin-A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 92.675477 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: GQFAVTNEEI KTASKIVRRV (SEP)NVEAFDKSG SVFKGYQIWT DISPTIENDP NIMFVKCVVQ QGSKKEKLTV VQIDPP GTG TPYDIDPTHA WNCNSQVDPM SFGDIGLLNH TNIPCVLDFL KHRYLKNQIY TTAVPLIVAI NPYKDLGNTT NEWIRRY RD TADHTKLPPH ...String: GQFAVTNEEI KTASKIVRRV (SEP)NVEAFDKSG SVFKGYQIWT DISPTIENDP NIMFVKCVVQ QGSKKEKLTV VQIDPP GTG TPYDIDPTHA WNCNSQVDPM SFGDIGLLNH TNIPCVLDFL KHRYLKNQIY TTAVPLIVAI NPYKDLGNTT NEWIRRY RD TADHTKLPPH VFTCAREALS NLHGVNKSQT IIVSGESGAG KTEATKQIMR YFASSKSGNM DLRIQTAIMA ANPVLEAF G NAKTIRNNNS SRFGRFMQLV ISHEGGIRYG SVVAFLLEKS RIITQDDNER SYHIFYQFLK GANSTMKSKF GLKGVTEYK LLNPNSTEVS GVDDVKDFEE VIESLKNMEL SESDIEVIFS IVAGILTLGN VRLIEKQEAG LSDAAAIMDE DMGVFNKACE LMYLDPELI KREILIKVTV AGGTKIEGRW NKNDAEVLKS SLCKAMYEKL FLWIIRHLNS RIEPEGGFKT FMGMLDIFGF E VFKNNSLE QLFINITNEM LQKNFVDIVF ERESKLYKDE GISTAELKYT SNKEVINVLC EKGKSVLSYL EDQCLAPGGT DE KFVSSCA TNLKENNKFT PAKVASNKNF IIQHTIGPIQ YCAESFLLKN KDVLRGDLVE VIKDSPNPIV QQLFEGQVIE KGK IAKGSL IGSQFLNQLT SLMNLINSTE PHFIRCIKPN ENKKPLEWCE PKILIQLHAL SILEALVLRQ LGYSYRRTFE EFLY QYKFV DIAAAEDSSV ENQNKCVNIL KLSGLSESMY KIGKSMVFLK QEGAKILTKI QREKLVEWEN CVSVIEAAIL KHKYK QKVN KNIPSLLRVQ AHIRKKMVAQ |
-Macromolecule #2: Actin-1
Macromolecule | Name: Actin-1 / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO |
---|---|
Source (natural) | Organism: ![]() ![]() ![]() |
Molecular weight | Theoretical: 42.047676 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: GAMGEEDVQA LVVDNGSGNV KAGVAGDDAP RSVFPSIVGR PKNPGIMVGM EEKDAFVGDE AQTKRGILTL KYPIEHGIVT NWDDMEKIW HHTFYNELRA APEEHPVLLT EAPLNPKGNR ERMTQIMFES FNVPAMYVAI QAVLSLYSSG RTTGIVLDSG D GVSHTVPI ...String: GAMGEEDVQA LVVDNGSGNV KAGVAGDDAP RSVFPSIVGR PKNPGIMVGM EEKDAFVGDE AQTKRGILTL KYPIEHGIVT NWDDMEKIW HHTFYNELRA APEEHPVLLT EAPLNPKGNR ERMTQIMFES FNVPAMYVAI QAVLSLYSSG RTTGIVLDSG D GVSHTVPI YEGYALPHAI MRLDLAGRDL TEYLMKILHE RGYGFSTSAE KEIVRDIKEK LCYIALNFDE EMKTSEQSSD IE KSYELPD GNIITVGNER FRCPEALFQP SFLGKEAAGI HTTTFNSIKK CDVDIRKDLY GNIVLSGGTT MYEGIGERLT RDI TTLAPS TMKIKVVAPP ERKYSVWIGG SILSSLSTFQ QMWITKEEYD ESGPSIVHRK CF |
-Macromolecule #3: ADENOSINE-5'-DIPHOSPHATE
Macromolecule | Name: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 4 / Formula: ADP |
---|---|
Molecular weight | Theoretical: 427.201 Da |
Chemical component information | ![]() ChemComp-ADP: |
-Macromolecule #4: MAGNESIUM ION
Macromolecule | Name: MAGNESIUM ION / type: ligand / ID: 4 / Number of copies: 4 / Formula: MG |
---|---|
Molecular weight | Theoretical: 24.305 Da |
-Macromolecule #5: Jasplakinolide
Macromolecule | Name: Jasplakinolide / type: ligand / ID: 5 / Number of copies: 4 / Formula: 9UE |
---|---|
Molecular weight | Theoretical: 709.67 Da |
Chemical component information | ![]() ChemComp-9UE: |
-Experimental details
-Structure determination
Method | ![]() |
---|---|
![]() | helical reconstruction |
Aggregation state | filament |
-
Sample preparation
Buffer | pH: 7.5 |
---|---|
Vitrification | Cryogen name: ETHANE |
-
Electron microscopy
Microscope | FEI TITAN KRIOS |
---|---|
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Average electron dose: 49.2 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
-
Image processing
Startup model | Type of model: OTHER / Details: a cylinder |
---|---|
Final angle assignment | Type: NOT APPLICABLE |
Final reconstruction | Applied symmetry - Helical parameters - Δz: 28.3417 Å Applied symmetry - Helical parameters - Δ&Phi: -166.498 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.0 beta) / Number images used: 239021 |