+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-29936 | |||||||||
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Title | CRYO-EM STRUCTURE OF IMPORTIN ALPHA1/BETA HETERODIMER | |||||||||
Map data | ||||||||||
Sample |
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Keywords | Importins / TRANSPORT PROTEIN | |||||||||
Function / homology | Function and homology information RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / Sensing of DNA Double Strand Breaks / endoplasmic reticulum tubular network / regulation of DNA recombination / establishment of mitotic spindle localization / astral microtubule organization / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle ...RNA import into nucleus / Inhibition of nitric oxide production / mitotic chromosome movement towards spindle pole / Sensing of DNA Double Strand Breaks / endoplasmic reticulum tubular network / regulation of DNA recombination / establishment of mitotic spindle localization / astral microtubule organization / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / Transport of Ribonucleoproteins into the Host Nucleus / Regulation of cholesterol biosynthesis by SREBP (SREBF) / ribosomal protein import into nucleus / importin-alpha family protein binding / Initiation of Nuclear Envelope (NE) Reformation / NS1 Mediated Effects on Host Pathways / NLS-dependent protein nuclear import complex / Apoptosis induced DNA fragmentation / Nuclear import of Rev protein / Postmitotic nuclear pore complex (NPC) reformation / CREB1 phosphorylation through the activation of CaMKII/CaMKK/CaMKIV cascasde / nuclear import signal receptor activity / CaMK IV-mediated phosphorylation of CREB / nuclear localization sequence binding / DNA metabolic process / mitotic metaphase chromosome alignment / NLS-bearing protein import into nucleus / mitotic spindle assembly / positive regulation of type I interferon production / nuclear pore / Assembly of the ORC complex at the origin of replication / host cell / Hsp90 protein binding / ISG15 antiviral mechanism / small GTPase binding / histone deacetylase binding / cytoplasmic stress granule / specific granule lumen / protein import into nucleus / SARS-CoV-1 activates/modulates innate immune responses / Interferon alpha/beta signaling / nuclear envelope / nuclear membrane / Estrogen-dependent gene expression / ficolin-1-rich granule lumen / protein domain specific binding / Golgi membrane / Neutrophil degranulation / endoplasmic reticulum membrane / SARS-CoV-2 activates/modulates innate and adaptive immune responses / enzyme binding / RNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / membrane / nucleus / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.95 Å | |||||||||
Authors | Ko Y / Cingolani G | |||||||||
Funding support | United States, 1 items
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Citation | Journal: To Be Published Title: CRYO-EM STRUCTURE OF IMPORTIN ALPHA1/BETA HETERODIMER Authors: Ko Y / Cingolani G | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_29936.map.gz | 16.9 MB | EMDB map data format | |
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Header (meta data) | emd-29936-v30.xml emd-29936.xml | 14 KB 14 KB | Display Display | EMDB header |
Images | emd_29936.png | 104 KB | ||
Filedesc metadata | emd-29936.cif.gz | 5.5 KB | ||
Others | emd_29936_half_map_1.map.gz emd_29936_half_map_2.map.gz | 31.9 MB 31.9 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-29936 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-29936 | HTTPS FTP |
-Validation report
Summary document | emd_29936_validation.pdf.gz | 686.3 KB | Display | EMDB validaton report |
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Full document | emd_29936_full_validation.pdf.gz | 685.9 KB | Display | |
Data in XML | emd_29936_validation.xml.gz | 10.9 KB | Display | |
Data in CIF | emd_29936_validation.cif.gz | 12.6 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29936 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-29936 | HTTPS FTP |
-Related structure data
Related structure data | 8gcnMC 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_29936.map.gz / Format: CCP4 / Size: 34.3 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 0.872 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_29936_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_29936_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Importin Alpha1/Beta Heterodimer
Entire | Name: Importin Alpha1/Beta Heterodimer |
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Components |
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-Supramolecule #1: Importin Alpha1/Beta Heterodimer
Supramolecule | Name: Importin Alpha1/Beta Heterodimer / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: Importin subunit beta-1
Macromolecule | Name: Importin subunit beta-1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 97.257812 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARR EVKNYVLQTL GTETYRPSSA SQCVAGIACA EIPVNQWPEL IPQLVANVTN PNSTEHMKES TLEAIGYICQ D IDPEQLQD ...String: MELITILEKT VSPDRLELEA AQKFLERAAV ENLPTFLVEL SRVLANPGNS QVARVAAGLQ IKNSLTSKDP DIKAQYQQRW LAIDANARR EVKNYVLQTL GTETYRPSSA SQCVAGIACA EIPVNQWPEL IPQLVANVTN PNSTEHMKES TLEAIGYICQ D IDPEQLQD KSNEILTAII QGMRKEEPSN NVKLAATNAL LNSLEFTKAN FDKESERHFI MQVVCEATQC PDTRVRVAAL QN LVKIMSL YYQYMETYMG PALFAITIEA MKSDIDEVAL QGIEFWSNVC DEEMDLAIEA SEAAEQGRPP EHTSKFYAKG ALQ YLVPIL TQTLTKQDEN DDDDDWNPCK AAGVCLMLLA TCCEDDIVPH VLPFIKEHIK NPDWRYRDAA VMAFGCILEG PEPS QLKPL VIQAMPTLIE LMKDPSVVVR DTAAWTVGRI CELLPEAAIN DVYLAPLLQC LIEGLSAEPR VASNVCWAFS SLAEA AYEA ADVADDQEEP ATYCLSSSFE LIVQKLLETT DRPDGHQNNL RSSAYESLME IVKNSAKDCY PAVQKTTLVI MERLQQ VLQ MESHIQSTSD RIQFNDLQSL LCATLQNVLR KVQHQDALQI SDVVMASLLR MFQSTAGSGG VQEDALMAVS TLVEVLG GE FLKYMEAFKP FLGIGLKNYA EYQVCLAAVG LVGDLCRALQ SNIIPFCDEV MQLLLENLGN ENVHRSVKPQ ILSVFGDI A LAIGGEFKKY LEVVLNTLQQ ASQAQVDKSD YDMVDYLNEL RESCLEAYTG IVQGLKGDQE NVHPDVMLVQ PRVEFILSF IDHIAGDEDH TDGVVACAAG LIGDLCTAFG KDVLKLVEAR PMIHELLTEG RRSKTNKAKT LATWATKELR KLKNQA UniProtKB: Importin subunit beta-1 |
-Macromolecule #2: Importin subunit alpha-1
Macromolecule | Name: Importin subunit alpha-1 / 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: 5.296262 KDa |
Recombinant expression | Organism: Escherichia coli (E. coli) |
Sequence | String: AARLHRFKNK GKDSTEMRRR RIEVNVELRK AKKDDQMLKR RNV UniProtKB: Importin subunit alpha-1 |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.95 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 1009142 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |