[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

TitleStructural basis for the activation of the lipid scramblase TMEM16F.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6692, Year 2022
Publish dateNov 5, 2022
AuthorsMelanie Arndt / Carolina Alvadia / Monique S Straub / Vanessa Clerico Mosina / Cristina Paulino / Raimund Dutzler /
PubMed AbstractTMEM16F, a member of the conserved TMEM16 family, plays a central role in the initiation of blood coagulation and the fusion of trophoblasts. The protein mediates passive ion and lipid transport in ...TMEM16F, a member of the conserved TMEM16 family, plays a central role in the initiation of blood coagulation and the fusion of trophoblasts. The protein mediates passive ion and lipid transport in response to an increase in intracellular Ca. However, the mechanism of how the protein facilitates both processes has remained elusive. Here we investigate the basis for TMEM16F activation. In a screen of residues lining the proposed site of conduction, we identify mutants with strongly activating phenotype. Structures of these mutants determined herein by cryo-electron microscopy show major rearrangements leading to the exposure of hydrophilic patches to the membrane, whose distortion facilitates lipid diffusion. The concomitant opening of a pore promotes ion conduction in the same protein conformation. Our work has revealed a mechanism that is distinct for this branch of the family and that will aid the development of a specific pharmacology for a promising drug target.
External linksNat Commun / PubMed:36335104 / PubMed Central
MethodsEM (single particle)
Resolution2.93 - 3.49 Å
Structure data

EMDB-15913, PDB-8b8g:
Cryo-EM structure of Ca2+-free mTMEM16F F518H mutant in Digitonin
Method: EM (single particle) / Resolution: 3.39 Å

EMDB-15914, PDB-8b8j:
Cryo-EM structure of Ca2+-bound mTMEM16F F518H mutant in Digitonin
Method: EM (single particle) / Resolution: 2.96 Å

EMDB-15916, PDB-8b8k:
Cryo-EM structure of Ca2+-bound mTMEM16F N562A mutant in Digitonin closed/closed
Method: EM (single particle) / Resolution: 3.01 Å

EMDB-15917, PDB-8b8m:
Cryo-EM structure of Ca2+-bound mTMEM16F N562A mutant in Digitonin open/closed
Method: EM (single particle) / Resolution: 3.49 Å

EMDB-15919, PDB-8b8q:
Structure of mTMEM16F in lipid Nanodiscs in the presence of Ca2+
Method: EM (single particle) / Resolution: 2.94 Å

EMDB-15958, PDB-8bc0:
Cryo-EM structure of Ca2+-bound mTMEM16F F518A Q623A mutant in GDN open/closed
Method: EM (single particle) / Resolution: 3.09 Å

EMDB-15959, PDB-8bc1:
Cryo-EM Structure of Ca2+-bound mTMEM16F F518A_Q623A mutant in GDN
Method: EM (single particle) / Resolution: 2.93 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-P1O:
1,2-DIDECANOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / DDPC, phospholipid*YM

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / Lipid Transport / Lipid Scrambling / Ion Channel / Plasma Membrane / Blood Clotting / Exocytosis / Membrane Fusion / Lipid Scramblase / Blood Coagulation / Viral Entry / Cell Fusion

+
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