[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

TitleStructures and gating mechanisms of human bestrophin anion channels.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 3836, Year 2022
Publish dateJul 4, 2022
AuthorsAaron P Owji / Jiali Wang / Alec Kittredge / Zada Clark / Yu Zhang / Wayne A Hendrickson / Tingting Yang /
PubMed AbstractBestrophin-1 (Best1) and bestrophin-2 (Best2) are two members of the bestrophin family of calcium (Ca)-activated chloride (Cl) channels with critical involvement in ocular physiology and direct ...Bestrophin-1 (Best1) and bestrophin-2 (Best2) are two members of the bestrophin family of calcium (Ca)-activated chloride (Cl) channels with critical involvement in ocular physiology and direct pathological relevance. Here, we report cryo-EM structures of wild-type human Best1 and Best2 in various states at up to 1.8 Å resolution. Ca-bound Best1 structures illustrate partially open conformations at the two Ca-dependent gates of the channels, in contrast to the fully open conformations observed in Ca-bound Best2, which is in accord with the significantly smaller currents conducted by Best1 in electrophysiological recordings. Comparison of the closed and open states reveals a C-terminal auto-inhibitory segment (AS), which constricts the channel concentrically by wrapping around the channel periphery in an inter-protomer manner and must be released to allow channel opening. Our results demonstrate that removing the AS from Best1 and Best2 results in truncation mutants with similar activities, while swapping the AS between Best1 and Best2 results in chimeric mutants with swapped activities, underlying a key role of the AS in determining paralog specificity among bestrophins.
External linksNat Commun / PubMed:35789156 / PubMed Central
MethodsEM (single particle)
Resolution1.78 - 3.11 Å
Structure data

EMDB-27127, PDB-8d1e:
hBest2 1uM Ca2+ (Ca2+-bound) closed state
Method: EM (single particle) / Resolution: 1.78 Å

EMDB-27128, PDB-8d1f:
hBest2 5mM Ca2+ (Ca2+-bound) closed state
Method: EM (single particle) / Resolution: 1.82 Å

EMDB-27129, PDB-8d1g:
hBest2 Ca2+-bound open state
Method: EM (single particle) / Resolution: 2.07 Å

EMDB-27130, PDB-8d1h:
hBest2 Ca2+-unbound closed state
Method: EM (single particle) / Resolution: 1.94 Å

EMDB-27131, PDB-8d1i:
hBest1 1uM Ca2+ (Ca2+-bound) closed state
Method: EM (single particle) / Resolution: 1.82 Å

EMDB-27132, PDB-8d1j:
hBest1 5mM Ca2+ (Ca2+-bound) closed state
Method: EM (single particle) / Resolution: 2.05 Å

EMDB-27133, PDB-8d1k:
hBest1 Ca2+-bound partially open neck state
Method: EM (single particle) / Resolution: 2.28 Å

EMDB-27134, PDB-8d1l:
hBest1 Ca2+-bound partially open aperture state
Method: EM (single particle) / Resolution: 2.12 Å

EMDB-27135, PDB-8d1m:
hBest1 Ca2+-unbound closed state
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-27136, PDB-8d1n:
bBest2_345 Ca2+-bound open state
Method: EM (single particle) / Resolution: 1.93 Å

EMDB-27137, PDB-8d1o:
hBest1_345 Ca2+-bound open state
Method: EM (single particle) / Resolution: 2.44 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-MC3:
1,2-DIMYRISTOYL-RAC-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-DU0:
2-[2-[(1~{S},2~{S},4~{S},5'~{R},6~{R},7~{S},8~{R},9~{S},12~{S},13~{R},16~{S})-5',7,9,13-tetramethylspiro[5-oxapentacyclo[10.8.0.0^{2,9}.0^{4,8}.0^{13,18}]icos-18-ene-6,2'-oxane]-16-yl]oxyethyl]propane-1,3-diol

ChemComp-CL:
Unknown entry / Chloride

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • bos taurus (cattle)
KeywordsTRANSPORT PROTEIN / Ion channel / chloride channel / anion channel / pentamer

+
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