[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleOrigin and arrangement of actin filaments for gliding motility in apicomplexan parasites revealed by cryo-electron tomography.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 4800, Year 2023
Publish dateAug 9, 2023
AuthorsMatthew Martinez / Shrawan Kumar Mageswaran / Amandine Guérin / William David Chen / Cameron Parker Thompson / Sabine Chavin / Dominique Soldati-Favre / Boris Striepen / Yi-Wei Chang /
PubMed AbstractThe phylum Apicomplexa comprises important eukaryotic parasites that invade host tissues and cells using a unique mechanism of gliding motility. Gliding is powered by actomyosin motors that ...The phylum Apicomplexa comprises important eukaryotic parasites that invade host tissues and cells using a unique mechanism of gliding motility. Gliding is powered by actomyosin motors that translocate host-attached surface adhesins along the parasite cell body. Actin filaments (F-actin) generated by Formin1 play a central role in this critical parasitic activity. However, their subcellular origin, path and ultrastructural arrangement are poorly understood. Here we used cryo-electron tomography to image motile Cryptosporidium parvum sporozoites and reveal the cellular architecture of F-actin at nanometer-scale resolution. We demonstrate that F-actin nucleates at the apically positioned preconoidal rings and is channeled into the pellicular space between the parasite plasma membrane and the inner membrane complex in a conoid extrusion-dependent manner. Within the pellicular space, filaments on the inner membrane complex surface appear to guide the apico-basal flux of F-actin. F-actin concordantly accumulates at the basal end of the parasite. Finally, analyzing a Formin1-depleted Toxoplasma gondii mutant pinpoints the upper preconoidal ring as the conserved nucleation hub for F-actin in Cryptosporidium and Toxoplasma. Together, we provide an ultrastructural model for the life cycle of F-actin for apicomplexan gliding motility.
External linksNat Commun / PubMed:37558667 / PubMed Central
MethodsEM (tomography) / EM (subtomogram averaging)
Resolution30.0 - 65.0 Å
Structure data

EMDB-29753: Tomogram of an apical end of a Toxoplasma Gondii tachyzoite displaying an extruded conoid
Method: EM (tomography)

EMDB-29754: Cryptosporidium parvum sporozoite apical end
Method: EM (tomography)

EMDB-29755: Cryptosporidium parvum sporozoite basal end
Method: EM (tomography)

EMDB-29784: Subtomogram average of the preconoidal rings from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 35.0 Å

EMDB-29791: Refined subtomogram average of the top preconoidal ring from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 30.0 Å

EMDB-29801: Refined subtomogram average of the bottom preconoidal ring from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 35.0 Å

EMDB-29808: Subtomogram average of the IMC surface filaments, top view, from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 38.5 Å

EMDB-29809: IMC surface filament, sawtooth conformation, from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 47.0 Å

EMDB-29810: IMC surface filament, side view, from Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 53.0 Å

EMDB-29826: Upper preconoidal ring from Toxoplasma gondii tachyzoites
Method: EM (subtomogram averaging) / Resolution: 41.0 Å

EMDB-29827: Lower preconoidal ring of Toxoplasma gondii tachyzoites
Method: EM (subtomogram averaging) / Resolution: 41.0 Å

EMDB-29832: Preconoidal rings of Toxoplasma gondii tachyzoites
Method: EM (subtomogram averaging) / Resolution: 53.0 Å

EMDB-29835: Basal IMC pore of Cryptosporidium parvum sporozoites
Method: EM (subtomogram averaging) / Resolution: 65.0 Å

EMDB-29838: Preconoidal rings of Toxoplasma gondii tachyzoites with Formin1 conditionally depleted
Method: EM (subtomogram averaging) / Resolution: 50.0 Å

EMDB-29839: Upper preconoidal ring of Toxoplasma gondii tachyzoites with Formin1 conditionally depleted
Method: EM (subtomogram averaging) / Resolution: 38.0 Å

EMDB-29840: Lower preconoidal ring from Toxoplasma gondii tachyzoites with Formin1 conditionally depleted
Method: EM (subtomogram averaging) / Resolution: 44.0 Å

Source
  • Toxoplasma gondii (eukaryote)
  • Cryptosporidium parvum Iowa (eukaryote)

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more