[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 mechanisms of gating and selectivity of human rod CNGA1 channel.
Journal, issue, pagesNeuron, Vol. 109, Issue 8, Page 1302-11313.e4, Year 2021
Publish dateApr 21, 2021
AuthorsJing Xue / Yan Han / Weizhong Zeng / Yan Wang / Youxing Jiang /
PubMed AbstractMammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand ...Mammalian cyclic nucleotide-gated (CNG) channels play an essential role in the signal transduction of the visual and olfactory sensory systems. Here we reveal the structural mechanism of ligand gating in human rod CNGA1 channel by determining its cryo-EM structures in both the apo closed and cGMP-bound open states. Distinct from most other members of voltage-gated tetrameric cation channels, CNGA1 forms a central channel gate in the middle of the membrane, occluding the central cavity. Structural analyses of ion binding profiles in the selectivity filters of the wild-type channel and the E365Q filter mutant allow us to unambiguously define the two Ca binding sites inside the selectivity filter, providing structural insights into Ca blockage and permeation in CNG channels. The structure of the E365Q mutant also reveals two alternative side-chain conformations at Q365, providing a plausible explanation for the voltage-dependent gating of CNG channel acquired upon E365 mutation.
External linksNeuron / PubMed:33651975 / PubMed Central
MethodsEM (single particle)
Resolution2.6 - 3.6 Å
Structure data

23306

7lft

EMDB-23306, PDB-7lft:
Cryo-EM structure of human Apo CNGA1 channel in K+/Ca2+
Method: EM (single particle) / Resolution: 2.6 Å

23307

7lfw

EMDB-23307, PDB-7lfw:
Cryo-EM structure of human cGMP-bound open CNGA1 channel in K+/Ca2+
Method: EM (single particle) / Resolution: 2.9 Å

23308

7lfx

EMDB-23308, PDB-7lfx:
Cryo-EM structure of human cGMP-bound open CNGA1 channel in Na+/Ca2+
Method: EM (single particle) / Resolution: 3.1 Å

23309

7lfy

EMDB-23309, PDB-7lfy:
Cryo-EM structure of human cGMP-bound open CNGA1 channel in Na+
Method: EM (single particle) / Resolution: 3.6 Å

23310

7lg1

EMDB-23310, PDB-7lg1:
Cryo-EM structure of human cGMP-bound CNGA1_E365Q channel in Na+/Ca2+
Method: EM (single particle) / Resolution: 2.7 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL

ChemComp-CPL:
1-PALMITOYL-2-LINOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE / phospholipid*YM

ChemComp-K:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-PCG:
CYCLIC GUANOSINE MONOPHOSPHATE

ChemComp-CA:
Unknown entry

ChemComp-NA:
Unknown entry

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / ALPHA-HELICAL / ION CHANNEL

+
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://pdbjlvh1.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