+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-24757 | |||||||||
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Title | Insulin Degrading Enzyme pO/pC | |||||||||
Map data | Insulin Degrading Enzyme pO/pC | |||||||||
Sample |
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Function / homology | Function and homology information insulysin / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / ubiquitin-modified protein reader activity / insulin binding / negative regulation of NAD(P)H oxidase activity ...insulysin / ubiquitin recycling / insulin catabolic process / insulin metabolic process / amyloid-beta clearance by cellular catabolic process / hormone catabolic process / bradykinin catabolic process / ubiquitin-modified protein reader activity / insulin binding / negative regulation of NAD(P)H oxidase activity / regulation of aerobic respiration / negative regulation of glycogen catabolic process / regulation of cellular amino acid metabolic process / peptide catabolic process / Signaling by Insulin receptor / IRS activation / nitric oxide-cGMP-mediated signaling / Insulin processing / negative regulation of fatty acid metabolic process / negative regulation of feeding behavior / regulation of protein secretion / amyloid-beta clearance / positive regulation of peptide hormone secretion / Regulation of gene expression in beta cells / positive regulation of respiratory burst / peroxisomal matrix / alpha-beta T cell activation / negative regulation of acute inflammatory response / negative regulation of respiratory burst involved in inflammatory response / positive regulation of dendritic spine maintenance / Synthesis, secretion, and deacylation of Ghrelin / positive regulation of glycogen biosynthetic process / negative regulation of protein secretion / Signal attenuation / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / negative regulation of gluconeogenesis / positive regulation of nitric oxide mediated signal transduction / fatty acid homeostasis / regulation of protein localization to plasma membrane / amyloid-beta metabolic process / COPI-mediated anterograde transport / negative regulation of lipid catabolic process / positive regulation of lipid biosynthetic process / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / positive regulation of insulin receptor signaling pathway / negative regulation of reactive oxygen species biosynthetic process / transport vesicle / positive regulation of protein autophosphorylation / Insulin receptor recycling / insulin-like growth factor receptor binding / NPAS4 regulates expression of target genes / positive regulation of protein metabolic process / neuron projection maintenance / endoplasmic reticulum-Golgi intermediate compartment membrane / positive regulation of brown fat cell differentiation / activation of protein kinase B activity / positive regulation of glycolytic process / proteolysis involved in protein catabolic process / Insulin receptor signalling cascade / positive regulation of mitotic nuclear division / Regulation of insulin secretion / positive regulation of long-term synaptic potentiation / endosome lumen / positive regulation of cytokine production / acute-phase response / positive regulation of protein secretion / positive regulation of nitric-oxide synthase activity / regulation of transmembrane transporter activity / positive regulation of cell differentiation / Peroxisomal protein import / positive regulation of glucose import / peptide binding / negative regulation of proteolysis / regulation of synaptic plasticity / protein catabolic process / wound healing / insulin receptor binding / hormone activity / negative regulation of protein catabolic process / metalloendopeptidase activity / antigen processing and presentation of endogenous peptide antigen via MHC class I / cognition / positive regulation of neuron projection development / Golgi lumen / peroxisome / positive regulation of protein localization to nucleus / vasodilation / positive regulation of protein catabolic process / glucose metabolic process / regulation of protein localization / glucose homeostasis / virus receptor activity / cell-cell signaling / insulin receptor signaling pathway / positive regulation of NF-kappaB transcription factor activity / positive regulation of protein binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of cell growth / basolateral plasma membrane / secretory granule lumen Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.3 Å | |||||||||
Authors | Mancl JM / Liang WG / Tang WJ | |||||||||
Funding support | United States, 1 items
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Citation | Journal: To be published Title: Ensemble cryoEM reveals a substrate-induced shift in the conformational dynamics of human insulin degrading enzyme Authors: Mancl JM / Liang WG / Wei H / Carragher B / Potter CS / Tang WJ | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_24757.map.gz | 60 MB | EMDB map data format | |
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Header (meta data) | emd-24757-v30.xml emd-24757.xml | 12.9 KB 12.9 KB | Display Display | EMDB header |
Images | emd_24757.png | 46.2 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-24757 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-24757 | HTTPS FTP |
-Related structure data
Related structure data | 7rzeMC 7rzfC 7rzgC 7rzhC 7rziC M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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Related items in Molecule of the Month |
-Map
File | Download / File: emd_24757.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Annotation | Insulin Degrading Enzyme pO/pC | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.0842 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : Cysteine-free Insulin-degrading enzyme in complex with Insulin A ...
Entire | Name: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain |
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Components |
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-Supramolecule #1: Cysteine-free Insulin-degrading enzyme in complex with Insulin A ...
Supramolecule | Name: Cysteine-free Insulin-degrading enzyme in complex with Insulin A chain and Insulin B chain type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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-Supramolecule #2: Cysteine-free Insulin-degrading enzyme
Supramolecule | Name: Cysteine-free Insulin-degrading enzyme / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Escherichia coli (E. coli) |
-Supramolecule #3: Insulin A chain, Insulin B chain
Supramolecule | Name: Insulin A chain, Insulin B chain / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2-#3 |
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Source (natural) | Organism: Homo sapiens (human) |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
-Macromolecule #1: Cysteine-free Insulin-degrading enzyme
Macromolecule | Name: Cysteine-free Insulin-degrading enzyme / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: insulysin |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 117.068508 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAA LDVHIGSLSD PPNIAGLSHF LEHMLFLGTK KYPKENEYSQ FLSEHAGSSN AFTSGEHTNY YFDVSHEHLE G ALDRFAQF ...String: MRYRLAWLLH PALPSTFRSV LGARLPPPER LCGFQKKTYS KMNNPAIKRI GNHITKSPED KREYRGLELA NGIKVLLISD PTTDKSSAA LDVHIGSLSD PPNIAGLSHF LEHMLFLGTK KYPKENEYSQ FLSEHAGSSN AFTSGEHTNY YFDVSHEHLE G ALDRFAQF FLSPLFDESA KDREVNAVDS EHEKNVMNDA WRLFQLEKAT GNPKHPFSKF GTGNKYTLET RPNQEGIDVR QE LLKFHSA YYSSNLMAVV VLGRESLDDL TNLVVKLFSE VENKNVPLPE FPEHPFQEEH LKQLYKIVPI KDIRNLYVTF PIP DLQKYY KSNPGHYLGH LIGHEGPGSL LSELKSKGWV NTLVGGQKEG ARGFMFFIIN VDLTEEGLLH VEDIILHMFQ YIQK LRAEG PQEWVFQELK DLNAVAFRFK DKERPRGYTS KIAGILHYYP LEEVLTAEYL LEEFRPDLIE MVLDKLRPEN VRVAI VSKS FEGKTDRTEE WYGTQYKQEA IPDEVIKKWQ NADLNGKFKL PTKNEFIPTN FEILPLEKEA TPYPALIKDT AMSKLW FKQ DDKFFLPKAN LNFEFFSPFA YVDPLHSNMA YLYLELLKDS LNEYAYAAEL AGLSYDLQNT IYGMYLSVKG YNDKQPI LL KKIIEKMATF EIDEKRFEII KEAYMRSLNN FRAEQPHQHA MYYLRLLMTE VAWTKDELKE ALDDVTLPRL KAFIPQLL S RLHIEALLHG NITKQAALGI MQMVEDTLIE HAHTKPLLPS QLVRYREVQL PDRGWFVYQQ RNEVHNNSGI EIYYQTDMQ STSENMFLEL FAQIISEPAF NTLRTKEQLG YIVFSGPRRA NGIQGLRFII QSEKPPHYLE SRVEAFLITM EKSIEDMTEE AFQKHIQAL AIRRLDKPKK LSAESAKYWG EIISQQYNFD RDNTEVAYLK TLTKEDIIKF YKEMLAVDAP RRHKVSVHVL A REMDSSPV VGEFPSQNDI NLSQAPALPQ PEVIQNMTEF KRGLPLFPLV KPH |
-Macromolecule #2: Insulin A chain
Macromolecule | Name: Insulin A chain / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 2.383698 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: GIVEQCCTSI CSLYQLENYC N |
-Macromolecule #3: Insulin B chain
Macromolecule | Name: Insulin B chain / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 3.417931 KDa |
Recombinant expression | Organism: Saccharomyces cerevisiae (brewer's yeast) |
Sequence | String: FVNQHLCGSH LVEALYLVCG ERGFFYTPLT |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.2 |
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Vitrification | Cryogen name: ETHANE / Instrument: SPOTITON |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy |
Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2 |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
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Final angle assignment | Type: MAXIMUM LIKELIHOOD |
Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 76379 |