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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-6944 | |||||||||
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Title | Structure of human mitochondrial trifunctional protein, octamer | |||||||||
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![]() | fatty acid beta-oxidation / cryo-EM single-particle reconstruction / mitochondrial trifunctional protein / Liase / Oxidoreductase-Transferase complex | |||||||||
Function / homology | ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Liang K / Li N / Dai J / Wang X / Liu P / Chen X / Wang C / Gao N / Xiao J | |||||||||
![]() | ![]() Title: Cryo-EM structure of human mitochondrial trifunctional protein. Authors: Kai Liang / Ningning Li / Xiao Wang / Jianye Dai / Pulan Liu / Chu Wang / Xiao-Wei Chen / Ning Gao / Junyu Xiao / ![]() Abstract: The mitochondrial trifunctional protein (TFP) catalyzes three reactions in the fatty acid β-oxidation process. Mutations in the two TFP subunits cause mitochondrial trifunctional protein deficiency ...The mitochondrial trifunctional protein (TFP) catalyzes three reactions in the fatty acid β-oxidation process. Mutations in the two TFP subunits cause mitochondrial trifunctional protein deficiency and acute fatty liver of pregnancy that can lead to death. Here we report a 4.2-Å cryo-electron microscopy α2β2 tetrameric structure of the human TFP. The tetramer has a V-shaped architecture that displays a distinct assembly compared with the bacterial TFPs. A concave surface of the TFP tetramer interacts with the detergent molecules in the structure, suggesting that this region is involved in associating with the membrane. Deletion of a helical hairpin in TFPβ decreases its binding to the liposomes in vitro and reduces its membrane targeting in cells. Our results provide the structural basis for TFP function and have important implications for fatty acid oxidation related diseases. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 917.9 KB | ![]() | |
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Header (meta data) | ![]() ![]() | 12.1 KB 12.1 KB | Display Display | ![]() |
Images | ![]() | 234.4 KB | ||
Filedesc metadata | ![]() | 5.8 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5zrvMC ![]() 6940C ![]() 6945C ![]() 5zqzC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 2.64 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : human mitochondrial trifunctional protein
Entire | Name: human mitochondrial trifunctional protein |
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Components |
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-Supramolecule #1: human mitochondrial trifunctional protein
Supramolecule | Name: human mitochondrial trifunctional protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() ![]() |
-Macromolecule #1: Trifunctional enzyme subunit alpha, mitochondrial
Macromolecule | Name: Trifunctional enzyme subunit alpha, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 4 / Enantiomer: LEVO / EC number: ![]() |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 83.112625 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA VVRINSPNSK VNTLSKELHS EFSEVMNEIW ASDQIRSAV LISSKPGCFI AGADINMLAA CKTLQEVTQL SQEAQRIVEK LEKSTKPIVA AINGSCLGGG LEVAISCQYR I ATKDRKTV ...String: MVACRAIGIL SRFSAFRILR SRGYICRNFT GSSALLTRTH INYGVKGDVA VVRINSPNSK VNTLSKELHS EFSEVMNEIW ASDQIRSAV LISSKPGCFI AGADINMLAA CKTLQEVTQL SQEAQRIVEK LEKSTKPIVA AINGSCLGGG LEVAISCQYR I ATKDRKTV LGTPEVLLGA LPGAGGTQRL PKMVGVPAAL DMMLTGRSIR ADRAKKMGLV DQLVEPLGPG LKPPEERTIE YL EEVAITF AKGLADKKIS PKRDKGLVEK LTAYAMTIPF VRQQVYKKVE EKVRKQTKGL YPAPLKIIDV VKTGIEQGSD AGY LCESQK FGELVMTKES KALMGLYHGQ VLCKKNKFGA PQKDVKHLAI LGAGLMGAGI AQVSVDKGLK TILKDATLTA LDRG QQQVF KGLNDKVKKK ALTSFERDSI FSNLTGQLDY QGFEKADMVI EAVFEDLSLK HRVLKEVEAV IPDHCIFASN TSALP ISEI AAVSKRPEKV IGMHYFSPVD KMQLLEIITT EKTSKDTSAS AVAVGLKQGK VIIVVKDGPG FYTTRCLAPM MSEVIR ILQ EGVDPKKLDS LTTSFGFPVG AATLVDEVGV DVAKHVAEDL GKVFGERFGG GNPELLTQMV SKGFLGRKSG KGFYIYQ EG VKRKDLNSDM DSILASLKLP PKSEVSSDED IQFRLVTRFV NEAVMCLQEG ILATPAEGDI GAVFGLGFPP CLGGPFRF V DLYGAQKIVD RLKKYEAAYG KQFTPCQLLA DHANSPNKKF YQ UniProtKB: Trifunctional enzyme subunit alpha, mitochondrial |
-Macromolecule #2: Trifunctional enzyme subunit beta, mitochondrial
Macromolecule | Name: Trifunctional enzyme subunit beta, mitochondrial / type: protein_or_peptide / ID: 2 / Number of copies: 4 / Enantiomer: LEVO / EC number: ![]() |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 51.360359 KDa |
Recombinant expression | Organism: ![]() ![]() ![]() |
Sequence | String: MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLH RTSVPKEVVD YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SANQAMTTGV GLIASGQCDV I VAGGVELM ...String: MTILTYPFKN LPTASKWALR FSIRPLSCSS QLRAAPAVQT KTKKTLAKPN IRNVVVVDGV RTPFLLSGTS YKDLMPHDLA RAALTGLLH RTSVPKEVVD YIIFGTVIQE VKTSNVAREA ALGAGFSDKT PAHTVTMACI SANQAMTTGV GLIASGQCDV I VAGGVELM SDVPIRHSRK MRKLMLDLNK AKSMGQRLSL ISKFRFNFLA PELPAVSEFS TSETMGHSAD RLAAAFAVSR LE QDEYALR SHSLAKKAQD EGLLSDVVPF KVPGKDTVTK DNGIRPSSLE QMAKLKPAFI KPYGTVTAAN SSFLTDGASA MLI MAEEKA LAMGYKPKAY LRDFMYVSQD PKDQLLLGPT YATPKVLEKA GLTMNDIDAF EFHEAFSGQI LANFKAMDSD WFAE NYMGR KTKVGLPPLE KFNNWGGSLS LGHPFGATGC RLVMAAANRL RKEGGQYGLV AACAAGGQGH AMIVEAYPK UniProtKB: Trifunctional enzyme subunit beta, mitochondrial |
-Experimental details
-Structure determination
Method | ![]() |
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Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Grid | Material: GOLD |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD![]() |
Image recording | Film or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2 |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 7.7 Å / Resolution method: FSC 0.143 CUT-OFF / Details: Gold Standard / Number images used: 48564 |