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- EMDB-0923: Cryo-EM structure of the CALHM chimeric construct (9-mer) -

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Basic information

Entry
Database: EMDB / ID: EMD-0923
TitleCryo-EM structure of the CALHM chimeric construct (9-mer)
Map datahalf map 2
Sample
  • Complex: CALHM
    • Protein or peptide: Calcium homeostasis modulator 1,Calcium homeostasis modulator protein 2
Keywordschannel / MEMBRANE PROTEIN
Function / homology
Function and homology information


regulation of microglial cell activation / ATP export / calcium ion import / monoatomic cation channel activity / regulation of synaptic plasticity / calcium channel activity / basolateral plasma membrane / positive regulation of apoptotic process / endoplasmic reticulum membrane / plasma membrane
Similarity search - Function
Calcium homeostasis modulator family / Calcium homeostasis modulator
Similarity search - Domain/homology
Calcium homeostasis modulator 1 / Calcium homeostasis modulator protein 2
Similarity search - Component
Biological speciesOryzias latipes (Japanese medaka) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsDemura K / Kusakizako T
CitationJournal: Sci Adv / Year: 2020
Title: Cryo-EM structures of calcium homeostasis modulator channels in diverse oligomeric assemblies.
Authors: Kanae Demura / Tsukasa Kusakizako / Wataru Shihoya / Masahiro Hiraizumi / Kengo Nomura / Hiroto Shimada / Keitaro Yamashita / Tomohiro Nishizawa / Akiyuki Taruno / Osamu Nureki /
Abstract: Calcium homeostasis modulator (CALHM) family proteins are Ca-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we ...Calcium homeostasis modulator (CALHM) family proteins are Ca-regulated adenosine triphosphate (ATP)-release channels involved in neural functions including neurotransmission in gustation. Here, we present the cryo-electron microscopy (EM) structures of killifish CALHM1, human CALHM2, and CLHM-1 at resolutions of 2.66, 3.4, and 3.6 Å, respectively. The CALHM1 octamer structure reveals that the N-terminal helix forms the constriction site at the channel pore in the open state and modulates the ATP conductance. The CALHM2 undecamer and CLHM-1 nonamer structures show the different oligomeric stoichiometries among CALHM homologs. We further report the cryo-EM structures of the chimeric construct, revealing that the intersubunit interactions at the transmembrane domain (TMD) and the TMD-intracellular domain linker define the oligomeric stoichiometry. These findings advance our understanding of the ATP conduction and oligomerization mechanisms of CALHM channels.
History
DepositionDec 26, 2019-
Header (metadata) releaseJul 29, 2020-
Map releaseJul 29, 2020-
UpdateOct 23, 2024-
Current statusOct 23, 2024Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6lmx
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0923.png

Downloads & links

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Map

FileDownload / File: emd_0923.map.gz / Format: CCP4 / Size: 23 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationhalf map 2
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.41 Å/pix.
x 182 pix.
= 257.301 Å		1.41 Å/pix.
x 182 pix.
= 257.301 Å		1.41 Å/pix.
x 182 pix.
= 257.301 Å

Surface

Projections

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Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.41374 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.035 / Movie #1: 0.035
Minimum - Maximum-0.23514119 - 0.4013985
Average (Standard dev.)0.00044412725 (±0.0097787)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions182182182
Spacing182182182
CellA=B=C: 257.3007 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.41374175824181.41374175824181.4137417582418
M x/y/z182182182
origin x/y/z0.0000.0000.000
length x/y/z257.301257.301257.301
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS182182182
D min/max/mean-0.2350.4010.000

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Supplemental data

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Mask #1

Fileemd_0923_msk_1.map
Projections & Slices
AxesZYX

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Half map: half map 1

Fileemd_0923_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_0923_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

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Histogram

Histogram (log scale)

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Sample components

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Entire : CALHM

EntireName: CALHM
Components
  • Complex: CALHM
    • Protein or peptide: Calcium homeostasis modulator 1,Calcium homeostasis modulator protein 2

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Supramolecule #1: CALHM

SupramoleculeName: CALHM / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Oryzias latipes (Japanese medaka)

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Macromolecule #1: Calcium homeostasis modulator 1,Calcium homeostasis modulator pro...

MacromoleculeName: Calcium homeostasis modulator 1,Calcium homeostasis modulator protein 2
type: protein_or_peptide / ID: 1 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.417203 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDKFRMMFQF LQSNQESFMN GICGIMALAS AQMYSSFEFS CPCMPEYNYT YGIGLLIIPP IWFFLLGFVL NNNVSVLAEE WKRPTGRRT KDPSVLRYML CSITQRSLIA PAVWVSVTLM DGKSFLCAFS INLDIEKFGN ASLVIGMTET EKLKFLARIP C KDLFEDNE ...String:
MDKFRMMFQF LQSNQESFMN GICGIMALAS AQMYSSFEFS CPCMPEYNYT YGIGLLIIPP IWFFLLGFVL NNNVSVLAEE WKRPTGRRT KDPSVLRYML CSITQRSLIA PAVWVSVTLM DGKSFLCAFS INLDIEKFGN ASLVIGMTET EKLKFLARIP C KDLFEDNE VRVAATRYIK CISQACGWMF LLMMTFTAFL IRAIRPCFTQ ASYRQEAYWA QYRANEDQLF QRTAEVHSRV LA ANNVRRF FGFVALNKDD EELIANFPVE GTQPRPQWNA ITGVYLYREN QGLPLYSRLH KWAQGLAGNG AAPDNVEMAL LPS ENLYFQ

UniProtKB: Calcium homeostasis modulator 1, Calcium homeostasis modulator protein 2

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 227781
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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