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- EMDB-21142: Cryo-EM structure of an undecameric chicken CALHM1 and human CALH... -

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Basic information

Entry
Database: EMDB / ID: EMD-21142
TitleCryo-EM structure of an undecameric chicken CALHM1 and human CALHM2 chimera
Map datasharpened map of a chicken CALHM1 and human CALHM2 chimera
Sample
  • Complex: chimera of chicken CALHM1 and human CALHM2
    • Protein or peptide: Green fluorescent protein, CALHM1,CALMH2 chimera
Function / homology
Function and homology information


voltage-gated monoatomic ion channel activity / calcium-activated cation channel activity / monoatomic cation channel activity / bioluminescence / generation of precursor metabolites and energy / positive regulation of apoptotic process / membrane / plasma membrane
Similarity search - Function
Calcium homeostasis modulator protein 1 / Calcium homeostasis modulator family / Calcium homeostasis modulator / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein
Similarity search - Domain/homology
Calcium homeostasis modulator 1 / Green fluorescent protein / Calcium homeostasis modulator protein 2
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.87 Å
AuthorsSyrjanen JL / Chou TH / Furukawa H
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS) United States
National Institutes of Health/National Institute of Mental Health (NIH/NIMH)
CitationJournal: Nat Struct Mol Biol / Year: 2020
Title: Structure and assembly of calcium homeostasis modulator proteins.
Authors: Johanna L Syrjanen / Kevin Michalski / Tsung-Han Chou / Timothy Grant / Shanlin Rao / Noriko Simorowski / Stephen J Tucker / Nikolaus Grigorieff / Hiro Furukawa /
Abstract: The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap ...The biological membranes of many cell types contain large-pore channels through which a wide variety of ions and metabolites permeate. Examples include connexin, innexin and pannexin, which form gap junctions and/or bona fide cell surface channels. The most recently identified large-pore channels are the calcium homeostasis modulators (CALHMs), through which ions and ATP permeate in a voltage-dependent manner to control neuronal excitability, taste signaling and pathologies of depression and Alzheimer's disease. Despite such critical biological roles, the structures and patterns of their oligomeric assembly remain unclear. Here, we reveal the structures of two CALHMs, chicken CALHM1 and human CALHM2, by single-particle cryo-electron microscopy (cryo-EM), which show novel assembly of the four transmembrane helices into channels of octamers and undecamers, respectively. Furthermore, molecular dynamics simulations suggest that lipids can favorably assemble into a bilayer within the larger CALHM2 pore, but not within CALHM1, demonstrating the potential correlation between pore size, lipid accommodation and channel activity.
History
DepositionDec 17, 2019-
Header (metadata) releaseJan 15, 2020-
Map releaseJan 29, 2020-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 2.82
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 2.82
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6val
  • Surface level: 2.82
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21142.png

Downloads & links

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Map

FileDownload / File: emd_21142.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationsharpened map of a chicken CALHM1 and human CALHM2 chimera
Voxel sizeX=Y=Z: 1.06 Å
Density
Contour LevelBy AUTHOR: 2.82 / Movie #1: 2.82
Minimum - Maximum-7.2877445 - 11.973792
Average (Standard dev.)0.072356366 (±0.5612433)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 271.36 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.061.061.06
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z271.360271.360271.360
α/β/γ90.00090.00090.000
start NX/NY/NZ-38-19-20
NX/NY/NZ858082
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-7.28811.9740.072

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Supplemental data

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Additional map: unsharpened map of a chicken CALHM1 and human CALHM2 chimera

Fileemd_21142_additional.map
Annotationunsharpened map of a chicken CALHM1 and human CALHM2 chimera
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : chimera of chicken CALHM1 and human CALHM2

EntireName: chimera of chicken CALHM1 and human CALHM2
Components
  • Complex: chimera of chicken CALHM1 and human CALHM2
    • Protein or peptide: Green fluorescent protein, CALHM1,CALMH2 chimera

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Supramolecule #1: chimera of chicken CALHM1 and human CALHM2

SupramoleculeName: chimera of chicken CALHM1 and human CALHM2 / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)

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Macromolecule #1: Green fluorescent protein, CALHM1,CALMH2 chimera

MacromoleculeName: Green fluorescent protein, CALHM1,CALMH2 chimera / type: protein_or_peptide / ID: 1 / Number of copies: 11 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 69.023617 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG AHHHHHHHHA AAMVSKGEEL FTGVVPILVE LDGDVNGHKF SVSGEGEGDA TYGKLTLKF ICTTGKLPVP WPTLVTTLTY GVQCFSRYPD HMKQHDFFKS AMPEGYVQER TIFFKDDGNY KTRAEVKFEG D TLVNRIEL ...String:
MWSHPQFEKG GGSGGGSGGS AWSHPQFEKG AHHHHHHHHA AAMVSKGEEL FTGVVPILVE LDGDVNGHKF SVSGEGEGDA TYGKLTLKF ICTTGKLPVP WPTLVTTLTY GVQCFSRYPD HMKQHDFFKS AMPEGYVQER TIFFKDDGNY KTRAEVKFEG D TLVNRIEL KGIDFKEDGN ILGHKLEYNY NSHNVYIMAD KQKNGIKVNF KIRHNIEDGS VQLADHYQQN TPIGDGPVLL PD NHYLSTQ SKLSKDPNEK RDHMVLLEFV TAAGITLGMD ELYKSGLRSG LVPRGSEFDK FRMVFQFLQS NQESFMSGIC GIM ALASAQ LYSAFDFNCP CLPRYNLAYG LGVLLVPPLI LFLLGFVLNN NVSMLAEEWR RPQGQRQKDA AVLRYMFCSM VQRA MIAPA VWVSVTLLDG KCITCAFCTS LPVEALGNAS HHGLPQGEVK RVLARIPCKE IYDGQELIAN EVAVRYLRCI SQALG WCFV LLMTTLAFLV RSLKHYCSPL SYRQEAYWAQ YRANEDQLFQ RTAEVHSRVL AANNVRRFFG FVALNKDDEE LIANFP VEG TQPRPQWNAI TGVYLYRENQ GLPLYSRLHK WAQGLAGNGA APDNVEMALL PS

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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: 7.5
GridDetails: unspecified
VitrificationCryogen name: ETHANE / Chamber humidity: 85 % / Chamber temperature: 288.15 K / Instrument: FEI VITROBOT MARK IV / Details: Blot for 4 sec before plunging.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 57.2 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Details: undecameric human CALHM2 and octameric chicken CALHM1
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.87 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cisTEM / Number images used: 123664

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