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- EMDB-31440: Cryo-EM structure of human TMEM120A in the CoASH-bound state -

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Basic information

Entry
Database: EMDB / ID: EMD-31440
TitleCryo-EM structure of human TMEM120A in the CoASH-bound state
Map data
Sample
  • Cell: transmembrane protein 120ATransmembrane protein
    • Protein or peptide: Transmembrane protein 120ATransmembrane protein
  • Ligand: COENZYME A
Function / homology
Function and homology information


protein heterooligomerization / nuclear inner membrane / fat cell differentiation / detection of mechanical stimulus involved in sensory perception of pain / monoatomic ion transmembrane transport / protein homooligomerization / monoatomic ion channel activity / membrane / plasma membrane
Similarity search - Function
Ion channel TACAN/TMEM120B / TMPIT-like protein
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.69 Å
AuthorsSong DF / Rong Y / Liu ZF
Funding support China, 3 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31925024 China
National Natural Science Foundation of China (NSFC)31670749 China
Chinese Academy of SciencesXDB37020101 China
CitationJournal: Elife / Year: 2021
Title: TMEM120A contains a specific coenzyme A-binding site and might not mediate poking- or stretch-induced channel activities in cells.
Authors: Yao Rong / Jinghui Jiang / Yiwei Gao / Jianli Guo / Danfeng Song / Wenhao Liu / Mingmin Zhang / Yan Zhao / Bailong Xiao / Zhenfeng Liu /
Abstract: TMEM120A, a member of the transmembrane protein 120 (TMEM120) family, has a pivotal function in adipocyte differentiation and metabolism, and may also contribute to sensing mechanical pain by ...TMEM120A, a member of the transmembrane protein 120 (TMEM120) family, has a pivotal function in adipocyte differentiation and metabolism, and may also contribute to sensing mechanical pain by functioning as an ion channel named TACAN. Here we report that expression of TMEM120A is not sufficient in mediating poking- or stretch-induced currents in cells and have solved cryo-electron microscopy (cryo-EM) structures of human TMEM120A (TMEM120A) in complex with an endogenous metabolic cofactor (coenzyme A, CoASH) and in the apo form. TMEM120A forms a symmetrical homodimer with each monomer containing an amino-terminal coiled-coil motif followed by a transmembrane domain with six membrane-spanning helices. Within the transmembrane domain, a CoASH molecule is hosted in a deep cavity and forms specific interactions with nearby amino acid residues. Mutation of a central tryptophan residue involved in binding CoASH dramatically reduced the binding affinity of TMEM120A with CoASH. TMEM120A exhibits distinct conformations at the states with or without CoASH bound. Our results suggest that TMEM120A may have alternative functional roles potentially involved in CoASH transport, sensing, or metabolism.
History
DepositionJun 17, 2021-
Header (metadata) releaseJun 30, 2021-
Map releaseJun 30, 2021-
UpdateJan 12, 2022-
Current statusJan 12, 2022Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.9
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.9
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7f3t
  • Surface level: 0.9
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_31440.png

Downloads & links

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Map

FileDownload / File: emd_31440.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.07 Å
Density
Contour LevelBy AUTHOR: 0.9 / Movie #1: 0.9
Minimum - Maximum-3.7993762 - 6.1441374
Average (Standard dev.)0.0027412558 (±0.10654238)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions256256256
Spacing256256256
CellA=B=C: 273.92 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.071.071.07
M x/y/z256256256
origin x/y/z0.0000.0000.000
length x/y/z273.920273.920273.920
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS256256256
D min/max/mean-3.7996.1440.003

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Supplemental data

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Sample components

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Entire : transmembrane protein 120A

EntireName: transmembrane protein 120ATransmembrane protein
Components
  • Cell: transmembrane protein 120ATransmembrane protein
    • Protein or peptide: Transmembrane protein 120ATransmembrane protein
  • Ligand: COENZYME A

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Supramolecule #1: transmembrane protein 120A

SupramoleculeName: transmembrane protein 120A / type: cell / ID: 1 / Parent: 0 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Transmembrane protein 120A

MacromoleculeName: Transmembrane protein 120A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.843578 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDYKDDDDKW SHPQFEKHHH HHHHHWSHPQ FEKQPPPPGP LGDCLRDWED LQQDFQNIQE THRLYRLKLE ELTKLQNNCT SSITRQKKR LQELALALKK CKPSLPAEAE GAAQELENQM KERQGLFFDM EAYLPKKNGL YLSLVLGNVN VTLLSKQAKF A YKDEYEKF ...String:
MDYKDDDDKW SHPQFEKHHH HHHHHWSHPQ FEKQPPPPGP LGDCLRDWED LQQDFQNIQE THRLYRLKLE ELTKLQNNCT SSITRQKKR LQELALALKK CKPSLPAEAE GAAQELENQM KERQGLFFDM EAYLPKKNGL YLSLVLGNVN VTLLSKQAKF A YKDEYEKF KLYLTIILIL ISFTCRFLLN SRVTDAAFNF LLVWYYCTLT IRESILINNG SRIKGWWVFH HYVSTFLSGV ML TWPDGLM YQKFRNQFLS FSMYQSFVQF LQYYYQSGCL YRLRALGERH TMDLTVEGFQ SWMWRGLTFL LPFLFFGHFW QLF NALTLF NLAQDPQCKE WQVLMCGFPF LLLFLGNFFT TLRVVHHKFH SQRHGSKKD

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Macromolecule #2: COENZYME A

MacromoleculeName: COENZYME A / type: ligand / ID: 2 / Number of copies: 2 / Formula: COA
Molecular weightTheoretical: 767.534 Da
Chemical component information

ChemComp-COA:
COENZYME A / Coenzyme A

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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
Component:
ConcentrationFormulaName
50.0 mMNaClSodium chloridesodium chloride
20.0 mMHEPES
protease inhibitor cocktail
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
DetailsThe protein is reconstituted in lipid nanodiscs

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 81000
Specialist opticsEnergy filter - Slit width: 20 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Number grids imaged: 2 / Number real images: 8148 / Average exposure time: 1.875 sec. / Average electron dose: 60.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: CTFFIND (ver. 4.1.10)
Startup modelType of model: OTHER / Details: generated by cryoSPARC
Initial angle assignmentType: COMMON LINE / Software - Name: cryoSPARC (ver. 3.1)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 3.1)
Final angle assignmentType: COMMON LINE / Software - Name: cryoSPARC (ver. 3.1)
Final reconstructionApplied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.69 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.1) / Number images used: 410963
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL / Target criteria: Correlation coefficient
Output model

PDB-7f3t:
Cryo-EM structure of human TMEM120A in the CoASH-bound state

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