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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Microsomal triglyceride transfer protein | |||||||||
![]() | Microsomal triglyceride transfer protein | |||||||||
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![]() | Microsomal triglyceride transfer protein / human liver / LIPID TRANSPORT / ISOMERASE / TRANSPORT PROTEIN | |||||||||
Function / homology | ![]() plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / phosphatidylcholine transfer activity / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing / triglyceride transport / interleukin-23-mediated signaling pathway ...plasma lipoprotein particle assembly / triglyceride transfer activity / chylomicron assembly / phosphatidylcholine transfer activity / regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / procollagen-proline 4-dioxygenase complex / VLDL assembly / insulin processing / triglyceride transport / interleukin-23-mediated signaling pathway / phosphatidylethanolamine transfer activity / phospholipid transfer activity / LDL remodeling / procollagen-proline 4-dioxygenase activity / thiol oxidase activity / protein disulfide-isomerase / ceramide 1-phosphate transfer activity / peptidyl-proline hydroxylation to 4-hydroxy-L-proline / very-low-density lipoprotein particle assembly / phospholipid transporter activity / endoplasmic reticulum chaperone complex / Collagen biosynthesis and modifying enzymes / protein folding in endoplasmic reticulum / lipid transporter activity / Chylomicron assembly / lipoprotein metabolic process / phospholipid transport / cholesterol transfer activity / Interleukin-23 signaling / low-density lipoprotein particle remodeling / interleukin-12-mediated signaling pathway / cellular response to interleukin-7 / Interleukin-12 signaling / lipoprotein transport / microvillus membrane / triglyceride metabolic process / protein disulfide isomerase activity / Insulin processing / Detoxification of Reactive Oxygen Species / apolipoprotein binding / endoplasmic reticulum-Golgi intermediate compartment / positive regulation of cell adhesion / protein secretion / protein-disulfide reductase activity / endoplasmic reticulum to Golgi vesicle-mediated transport / positive regulation of substrate adhesion-dependent cell spreading / response to endoplasmic reticulum stress / establishment of localization in cell / cholesterol homeostasis / Hedgehog ligand biogenesis / brush border membrane / Post-translational protein phosphorylation / lipid metabolic process / response to calcium ion / circadian rhythm / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / melanosome / integrin binding / protein folding / lamellipodium / actin binding / cellular response to hypoxia / basolateral plasma membrane / vesicle / positive regulation of viral entry into host cell / cytoskeleton / receptor complex / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / focal adhesion / lipid binding / protein-containing complex binding / Golgi apparatus / enzyme binding / endoplasmic reticulum / protein-containing complex / RNA binding / extracellular exosome / extracellular region / cytosol Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.07 Å | |||||||||
![]() | Zhang Z | |||||||||
Funding support | ![]()
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![]() | ![]() 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 |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 97.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.6 KB 17.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.9 KB | Display | ![]() |
Images | ![]() | 96.3 KB | ||
Filedesc metadata | ![]() | 5.9 KB | ||
Others | ![]() ![]() ![]() | 52.1 MB 95.6 MB 95.6 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 23.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8eojMC ![]() 7uzmC ![]() 8ekwC ![]() 8ekyC ![]() 8em2C ![]() 8emrC ![]() 8emsC ![]() 8emtC ![]() 8eneC ![]() 8eorC ![]() 23426 M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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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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Annotation | Microsomal triglyceride transfer protein | ||||||||||||||||||||
Voxel size | X=Y=Z: 1.08 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Additional map: Microsomal triglyceride transfer protein
File | emd_28377_additional_1.map | ||||||||||||
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Annotation | Microsomal triglyceride transfer protein | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Microsomal triglyceride transfer protein
File | emd_28377_half_map_1.map | ||||||||||||
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Annotation | Microsomal triglyceride transfer protein | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Microsomal triglyceride transfer protein
File | emd_28377_half_map_2.map | ||||||||||||
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Annotation | Microsomal triglyceride transfer protein | ||||||||||||
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Density Histograms |
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Sample components
-Entire : Microsomal triglyceride transfer protein
Entire | Name: Microsomal triglyceride transfer protein |
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Components |
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-Supramolecule #1: Microsomal triglyceride transfer protein
Supramolecule | Name: Microsomal triglyceride transfer protein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Protein disulfide-isomerase
Macromolecule | Name: Protein disulfide-isomerase / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: protein disulfide-isomerase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 57.190137 KDa |
Sequence | String: 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 |
-Macromolecule #2: Microsomal triglyceride transfer protein large subunit
Macromolecule | Name: Microsomal triglyceride transfer protein large subunit type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 99.474102 KDa |
Sequence | String: 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 |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 41.25 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination 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 |