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- EMDB-28377: Microsomal triglyceride transfer protein -

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Basic information

Entry
Database: EMDB / ID: EMD-28377
TitleMicrosomal triglyceride transfer protein
Map dataMicrosomal triglyceride transfer protein
Sample
  • Complex: Microsomal triglyceride transfer protein
    • Protein or peptide: Protein disulfide-isomerase
    • Protein or peptide: Microsomal triglyceride transfer protein large subunit
KeywordsMicrosomal triglyceride transfer protein / human liver / LIPID TRANSPORT / ISOMERASE / TRANSPORT PROTEIN
Function / homology
Function and homology information


plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / triglyceride transport / phosphatidylcholine transfer activity / procollagen-proline 4-dioxygenase complex / insulin processing / phosphatidylethanolamine transfer activity ...plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / triglyceride transport / phosphatidylcholine transfer activity / procollagen-proline 4-dioxygenase complex / insulin processing / phosphatidylethanolamine transfer activity / VLDL assembly / thiol oxidase activity / phospholipid transfer activity / procollagen-proline 4-dioxygenase activity / LDL remodeling / ceramide 1-phosphate transfer activity / protein disulfide-isomerase / very-low-density lipoprotein particle assembly / endoplasmic reticulum chaperone complex / phospholipid transporter activity / protein folding in endoplasmic reticulum / Collagen biosynthesis and modifying enzymes / lipid transporter activity / Chylomicron assembly / lipoprotein metabolic process / phospholipid transport / interleukin-23-mediated signaling pathway / cholesterol transfer activity / Interleukin-23 signaling / interleukin-12-mediated signaling pathway / low-density lipoprotein particle remodeling / Interleukin-12 signaling / cellular response to interleukin-7 / triglyceride metabolic process / lipoprotein transport / Insulin processing / protein disulfide isomerase activity / Detoxification of Reactive Oxygen Species / microvillus membrane / endoplasmic reticulum-Golgi intermediate compartment / protein-disulfide reductase activity / protein secretion / apolipoprotein binding / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of T cell migration / positive regulation of substrate adhesion-dependent cell spreading / positive regulation of cell adhesion / response to endoplasmic reticulum stress / cholesterol homeostasis / Post-translational protein phosphorylation / establishment of localization in cell / brush border membrane / Hedgehog ligand biogenesis / circadian rhythm / response to calcium ion / lipid metabolic process / integrin binding / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / melanosome / protein folding / lamellipodium / actin binding / basolateral plasma membrane / cellular response to hypoxia / vesicle / positive regulation of viral entry into host cell / cytoskeleton / receptor complex / endoplasmic reticulum lumen / protein heterodimerization activity / external side of plasma membrane / focal adhesion / lipid binding / protein-containing complex binding / enzyme binding / endoplasmic reticulum / Golgi apparatus / protein-containing complex / RNA binding / extracellular exosome / extracellular region / cytosol
Similarity search - Function
Microsomal triglyceride transfer protein large subunit / MTP large subunit, lipid-binding domain / MTP large subunit, lipid-binding domain / Vitellogenin, N-terminal / Lipovitellin-phosvitin complex, superhelical domain / Vitellinogen, beta-sheet N-terminal / Lipid transport protein, beta-sheet shell / Lipoprotein amino terminal region / Vitellogenin domain profile. / Lipoprotein N-terminal Domain ...Microsomal triglyceride transfer protein large subunit / MTP large subunit, lipid-binding domain / MTP large subunit, lipid-binding domain / Vitellogenin, N-terminal / Lipovitellin-phosvitin complex, superhelical domain / Vitellinogen, beta-sheet N-terminal / Lipid transport protein, beta-sheet shell / Lipoprotein amino terminal region / Vitellogenin domain profile. / Lipoprotein N-terminal Domain / Protein disulphide isomerase / Thioredoxin-like domain / Disulphide isomerase / Endoplasmic reticulum targeting sequence. / Thioredoxin / Thioredoxin, conserved site / Thioredoxin family active site. / Thioredoxin domain profile. / Thioredoxin domain / Thioredoxin-like superfamily
Similarity search - Domain/homology
Protein disulfide-isomerase / Microsomal triglyceride transfer protein large subunit
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.07 Å
AuthorsZhang Z
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID) United States
CitationJournal: Cell Rep / Year: 2023
Title: High-resolution structural-omics of human liver enzymes.
Authors: Chih-Chia Su / Meinan Lyu / Zhemin Zhang / Masaru Miyagi / Wei Huang / Derek J Taylor / Edward W Yu /
Abstract: We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined ...We applied raw human liver microsome lysate to a holey carbon grid and used cryo-electron microscopy (cryo-EM) to define its composition. From this sample we identified and simultaneously determined high-resolution structural information for ten unique human liver enzymes involved in diverse cellular processes. Notably, we determined the structure of the endoplasmic bifunctional protein H6PD, where the N- and C-terminal domains independently possess glucose-6-phosphate dehydrogenase and 6-phosphogluconolactonase enzymatic activity, respectively. We also obtained the structure of heterodimeric human GANAB, an ER glycoprotein quality-control machinery that contains a catalytic α subunit and a noncatalytic β subunit. In addition, we observed a decameric peroxidase, PRDX4, which directly contacts a disulfide isomerase-related protein, ERp46. Structural data suggest that several glycosylations, bound endogenous compounds, and ions associate with these human liver enzymes. These results highlight the importance of cryo-EM in facilitating the elucidation of human organ proteomics at the atomic level.
History
DepositionOct 3, 2022-
Header (metadata) releaseMay 3, 2023-
Map releaseMay 3, 2023-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28377.png

Downloads & links

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Map

FileDownload / File: emd_28377.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMicrosomal triglyceride transfer protein
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.08 Å/pix.
x 300 pix.
= 324. Å		1.08 Å/pix.
x 300 pix.
= 324. Å		1.08 Å/pix.
x 300 pix.
= 324. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.08 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-0.2886956 - 0.9311967
Average (Standard dev.)-0.0004139445 (±0.016373353)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 324.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Microsomal triglyceride transfer protein

Fileemd_28377_additional_1.map
AnnotationMicrosomal triglyceride transfer protein
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Microsomal triglyceride transfer protein

Fileemd_28377_half_map_1.map
AnnotationMicrosomal triglyceride transfer protein
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Microsomal triglyceride transfer protein

Fileemd_28377_half_map_2.map
AnnotationMicrosomal triglyceride transfer protein
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Microsomal triglyceride transfer protein

EntireName: Microsomal triglyceride transfer protein
Components
  • Complex: Microsomal triglyceride transfer protein
    • Protein or peptide: Protein disulfide-isomerase
    • Protein or peptide: Microsomal triglyceride transfer protein large subunit

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Supramolecule #1: Microsomal triglyceride transfer protein

SupramoleculeName: Microsomal triglyceride transfer protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Protein disulfide-isomerase

MacromoleculeName: Protein disulfide-isomerase / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: protein disulfide-isomerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 57.190137 KDa
SequenceString: MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESD LAQQYGVRGY PTIKFFRNGD TASPKEYTAG READDIVNWL KKRTGPAATT LPDGAAAESL VESSEVAVIG F FKDVESDS ...String:
MLRRALLCLA VAALVRADAP EEEDHVLVLR KSNFAEALAA HKYLLVEFYA PWCGHCKALA PEYAKAAGKL KAEGSEIRLA KVDATEESD LAQQYGVRGY PTIKFFRNGD TASPKEYTAG READDIVNWL KKRTGPAATT LPDGAAAESL VESSEVAVIG F FKDVESDS AKQFLQAAEA IDDIPFGITS NSDVFSKYQL DKDGVVLFKK FDEGRNNFEG EVTKENLLDF IKHNQLPLVI EF TEQTAPK IFGGEIKTHI LLFLPKSVSD YDGKLSNFKT AAESFKGKIL FIFIDSDHTD NQRILEFFGL KKEECPAVRL ITL EEEMTK YKPESEELTA ERITEFCHRF LEGKIKPHLM SQELPEDWDK QPVKVLVGKN FEDVAFDEKK NVFVEFYAPW CGHC KQLAP IWDKLGETYK DHENIVIAKM DSTANEVEAV KVHSFPTLKF FPASADRTVI DYNGERTLDG FKKFLESGGQ DGAGD DDDL EDLEEAEEPD MEEDDDQKAV KDEL

UniProtKB: Protein disulfide-isomerase

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Macromolecule #2: Microsomal triglyceride transfer protein large subunit

MacromoleculeName: Microsomal triglyceride transfer protein large subunit
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 99.474102 KDa
SequenceString: MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNV ENVNQQRGEK SIFKGKSPSK IMGKENLEAL QRPTLLHLIH GKVKEFYSYQ NEAVAIENIK RGLASLFQTQ L SSGTTNEV ...String:
MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNV ENVNQQRGEK SIFKGKSPSK IMGKENLEAL QRPTLLHLIH GKVKEFYSYQ NEAVAIENIK RGLASLFQTQ L SSGTTNEV DISGNCKVTY QAHQDKVIKI KALDSCKIAR SGFTTPNQVL GVSSKATSVT TYKIEDSFVI AVLAEETHNF GL NFLQTIK GKIVSKQKLE LKTTEAGPRL MSGKQAAAII KAVDSKYTAI PIVGQVFQSH CKGCPSLSEL WRSTRKYLQP DNL SKAEAV RNFLAFIQHL RTAKKEEILQ ILKMENKEVL PQLVDAVTSA QTSDSLEAIL DFLDFKSDSS IILQERFLYA CGFA SHPNE ELLRALISKF KGSIGSSDIR ETVMIITGTL VRKLCQNEGC KLKAVVEAKK LILGGLEKAE KKEDTRMYLL ALKNA LLPE GIPSLLKYAE AGEGPISHLA TTALQRYDLP FITDEVKKTL NRIYHQNRKV HEKTVRTAAA AIILNNNPSY MDVKNI LLS IGELPQEMNK YMLAIVQDIL RFEMPASKIV RRVLKEMVAH NYDRFSRSGS SSAYTGYIER SPRSASTYSL DILYSGS GI LRRSNLNIFQ YIGKAGLHGS QVVIEAQGLE ALIAATPDEG EENLDSYAGM SAILFDVQLR PVTFFNGYSD LMSKMLSA S GDPISVVKGL ILLIDHSQEL QLQSGLKANI EVQGGLAIDI SGAMEFSLWY RESKTRVKNR VTVVITTDIT VDSSFVKAG LETSTETEAG LEFISTVQFS QYPFLVCMQM DKDEAPFRQF EKKYERLSTG RGYVSQKRKE SVLAGCEFPL HQENSEMCKV VFAPQPDST SSGWF

UniProtKB: Microsomal triglyceride transfer protein large subunit

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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
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: 41.25 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.291 µm / Nominal defocus min: 0.17 µm / Nominal magnification: 81000
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 487553
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.07 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 249877
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION
FSC plot (resolution estimation)

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