[English] 日本語
Yorodumi
- EMDB-71821: Cryo-EM structure of NCLX at low pH (class 4b) -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-71821
TitleCryo-EM structure of NCLX at low pH (class 4b)
Map data
Sample
  • Complex: NCLX without Calcium
    • Protein or peptide: NCLX
KeywordsMembrane transporter / MEMBRANE PROTEIN
Function / homology
Function and homology information


calcium:sodium antiporter activity involved in regulation of cardiac muscle cell membrane potential / regulation of lymphocyte chemotaxis / Mitochondrial calcium ion transport / Sodium/Calcium exchangers / calcium export from the mitochondrion / calcium:sodium antiporter activity / mitochondrial calcium ion transmembrane transport / regulation of cardiac muscle cell membrane potential / mitochondrial calcium ion homeostasis / regulation of store-operated calcium entry ...calcium:sodium antiporter activity involved in regulation of cardiac muscle cell membrane potential / regulation of lymphocyte chemotaxis / Mitochondrial calcium ion transport / Sodium/Calcium exchangers / calcium export from the mitochondrion / calcium:sodium antiporter activity / mitochondrial calcium ion transmembrane transport / regulation of cardiac muscle cell membrane potential / mitochondrial calcium ion homeostasis / regulation of store-operated calcium entry / mitochondrial crista / regulation of cytosolic calcium ion concentration / regulation of insulin secretion / sodium ion transmembrane transport / sarcolemma / mitochondrial membrane / calcium ion transmembrane transport / intracellular calcium ion homeostasis / glucose homeostasis / mitochondrial inner membrane / protein homodimerization activity / mitochondrion / identical protein binding / membrane / plasma membrane
Similarity search - Function
: / Sodium/calcium exchanger membrane region / NCX, central ion-binding domain superfamily / Sodium/calcium exchanger protein
Similarity search - Domain/homology
Mitochondrial sodium/calcium exchanger protein
Similarity search - Component
Biological speciesHomo sapiens (human) / Rattus norvegicus (Norway rat)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.62 Å
AuthorsZhang J / Feng L
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS) United States
The G. Harold and Leila Y. Mathers Foundation United States
CitationJournal: Nature / Year: 2025
Title: Structure and mechanism of the mitochondrial calcium transporter NCLX.
Authors: Minrui Fan / Chen-Wei Tsai / Jinru Zhang / Jianxiu Zhang / Aswini R Krishnan / Tsung-Yun Liu / Yu-Lun Huang / Deniz Aydin / Siyuan Du / Briana L Sobecks / Madison X Rodriguez / Andrew H ...Authors: Minrui Fan / Chen-Wei Tsai / Jinru Zhang / Jianxiu Zhang / Aswini R Krishnan / Tsung-Yun Liu / Yu-Lun Huang / Deniz Aydin / Siyuan Du / Briana L Sobecks / Madison X Rodriguez / Andrew H Reiter / Carolyn R Bertozzi / Ron O Dror / Ming-Feng Tsai / Liang Feng /
Abstract: As a key mitochondrial Ca transporter, NCLX regulates intracellular Ca signalling and vital mitochondrial processes. The importance of NCLX in cardiac and nervous-system physiology is reflected by ...As a key mitochondrial Ca transporter, NCLX regulates intracellular Ca signalling and vital mitochondrial processes. The importance of NCLX in cardiac and nervous-system physiology is reflected by acute heart failure and neurodegenerative disorders caused by its malfunction. Despite substantial advances in the field, the transport mechanisms of NCLX remain unclear. Here we report the cryo-electron microscopy structures of NCLX, revealing its architecture, assembly, major conformational states and a previously undescribed mechanism for alternating access. Functional analyses further reveal an unexpected transport function of NCLX as a H/Ca exchanger, rather than as a Na/Ca exchanger as widely believed. These findings provide critical insights into mitochondrial Ca homeostasis and signalling, offering clues for developing therapies to treat diseases related to abnormal mitochondrial Ca.
History
DepositionJul 24, 2025-
Header (metadata) releaseSep 10, 2025-
Map releaseSep 10, 2025-
UpdateSep 24, 2025-
Current statusSep 24, 2025Processing site: RCSB / Status: Released

-
Structure visualization

Supplemental images

emd_71821.png

Downloads & links

-
Map

FileDownload / File: emd_71821.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.95 Å/pix.
x 320 pix.
= 304. Å		0.95 Å/pix.
x 320 pix.
= 304. Å		0.95 Å/pix.
x 320 pix.
= 304. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.95 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.23
Minimum - Maximum-1.4112868 - 2.0058675
Average (Standard dev.)-0.0003122603 (±0.0387323)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 304.0 Å
α=β=γ: 90.0 °

-
Supplemental data

-
Mask #1

Fileemd_71821_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #2

Fileemd_71821_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Half map: #1

Fileemd_71821_half_map_2.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

-
Sample components

-
Entire : NCLX without Calcium

EntireName: NCLX without Calcium
Components
  • Complex: NCLX without Calcium
    • Protein or peptide: NCLX

-
Supramolecule #1: NCLX without Calcium

SupramoleculeName: NCLX without Calcium / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

-
Macromolecule #1: NCLX

MacromoleculeName: NCLX / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 64.037688 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAGRWLDPLW APGFLCVALI LETASGAGDL STKAHGHIQF SARGVNQTAM ADCRAVCSLN TSDRCDFVKR NPDCHSEGGY LDYLKGIFC YFPPNLLPLA ITLYVFWLLY LFLILGVTAA KFFCPNLSAI STSLKLSHNV AGVTFLAFGN GAPDIFSALV A FSDPRTAG ...String:
MAGRWLDPLW APGFLCVALI LETASGAGDL STKAHGHIQF SARGVNQTAM ADCRAVCSLN TSDRCDFVKR NPDCHSEGGY LDYLKGIFC YFPPNLLPLA ITLYVFWLLY LFLILGVTAA KFFCPNLSAI STSLKLSHNV AGVTFLAFGN GAPDIFSALV A FSDPRTAG LAIGALFGAG VLVTTVVAGG ITILRPFMAA SRPFLRDITF YMVAVFLTFT ALYLGRITLV WALGYLGLYV FY VVTVIIC TWVYQRQRSR SLVHSISETP ELLTDSEEDQ MSSNTNSYDY GEEYRPLLLG EETTGQILLQ ALNPLDYRKW RTQ SISCKL LKVAKLPVEF LLLLTVPVVD PDKDDRNWKR PLNCLQLVIS PLVLVLTLQS GVYGIYEIGG LLPVWAVVVI VGTA LASVT FFATSNSEPP RLHWLFAFLG FLTSALWINA AATEVVNILR SLGVVFRLSN TVLGLTLLAW GNSIGDAFSD FTLAR QGYP RMAFSACFGG IIFNILVGVG LGCLLQIVRS HASEVKLEPD GLLVWVLASA LGLSLVFSLV SVPLQCFQLS KAYGLC LLL FYICFIVVVL LTEFGVIHLK AD

UniProtKB: Mitochondrial sodium/calcium exchanger protein

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON II (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 100.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: NONE
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.62 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 683191
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

+
About Yorodumi

-
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

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more