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- EMDB-31384: Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-106... -

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Basic information

Entry
Database: EMDB / ID: EMD-31384
TitleCryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution
Map dataCryo-EM single particle analysis of human Nup155 Longer N-terminus (19-1069)
Sample
  • Organelle or cellular component: Purified human Nup155 protein
    • Protein or peptide: G protein/GFP fusion protein,Nuclear pore complex protein Nup155
Function / homology
Function and homology information


nuclear pore inner ring / protein localization to nuclear inner membrane / nuclear envelope organization / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / atrial cardiac muscle cell action potential / Nuclear Pore Complex (NPC) Disassembly / Transport of Ribonucleoproteins into the Host Nucleus / miRNA processing / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) ...nuclear pore inner ring / protein localization to nuclear inner membrane / nuclear envelope organization / transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery / atrial cardiac muscle cell action potential / Nuclear Pore Complex (NPC) Disassembly / Transport of Ribonucleoproteins into the Host Nucleus / miRNA processing / Regulation of Glucokinase by Glucokinase Regulatory Protein / Defective TPR may confer susceptibility towards thyroid papillary carcinoma (TPC) / Transport of the SLBP independent Mature mRNA / Transport of the SLBP Dependant Mature mRNA / NS1 Mediated Effects on Host Pathways / SUMOylation of SUMOylation proteins / Transport of Mature mRNA Derived from an Intronless Transcript / RNA export from nucleus / structural constituent of nuclear pore / Rev-mediated nuclear export of HIV RNA / SUMOylation of RNA binding proteins / Nuclear import of Rev protein / Transport of Mature mRNA derived from an Intron-Containing Transcript / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / Viral Messenger RNA Synthesis / SUMOylation of ubiquitinylation proteins / Vpr-mediated nuclear import of PICs / SUMOylation of DNA replication proteins / Regulation of HSF1-mediated heat shock response / mRNA export from nucleus / SUMOylation of DNA damage response and repair proteins / nuclear pore / SUMOylation of chromatin organization proteins / bioluminescence / HCMV Late Events / generation of precursor metabolites and energy / Transcriptional regulation by small RNAs / ISG15 antiviral mechanism / HCMV Early Events / protein import into nucleus / nuclear envelope / snRNP Assembly / nuclear membrane / symbiont entry into host cell / viral envelope / virion attachment to host cell / SARS-CoV-2 activates/modulates innate and adaptive immune responses / membrane / cytosol
Similarity search - Function
Rhabdovirus glycoprotein / Rhabdovirus spike glycoprotein / Nucleoporin, Nup155-like, C-terminal, subdomain 3 / Nucleoporin, Nup155-like / Nucleoporin, Nup155-like, C-terminal, subdomain 1 / Nucleoporin, Nup155-like, C-terminal, subdomain 2 / Nucleoporin, Nup133/Nup155-like, N-terminal / Nup133 N terminal like / Green fluorescent protein, GFP / Green fluorescent protein-related ...Rhabdovirus glycoprotein / Rhabdovirus spike glycoprotein / Nucleoporin, Nup155-like, C-terminal, subdomain 3 / Nucleoporin, Nup155-like / Nucleoporin, Nup155-like, C-terminal, subdomain 1 / Nucleoporin, Nup155-like, C-terminal, subdomain 2 / Nucleoporin, Nup133/Nup155-like, N-terminal / Nup133 N terminal like / Green fluorescent protein, GFP / Green fluorescent protein-related / Green fluorescent protein / Green fluorescent protein
Similarity search - Domain/homology
G protein/GFP fusion protein / Nuclear pore complex protein Nup155
Similarity search - Component
Biological speciesRecombinant vesicular stomatitis Indiana virus rVSV-G/GFP / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 5.4 Å
AuthorsNiranjan S
Funding support India, 1 items
OrganizationGrant numberCountry
Department of Biotechnology (DBT, India)(DBT/PR/26398) India
CitationJournal: To Be Published
Title: Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution
Authors: Niranjan S
History
DepositionMay 31, 2021-
Header (metadata) releaseJun 8, 2022-
Map releaseJun 8, 2022-
UpdateJun 8, 2022-
Current statusJun 8, 2022Processing site: PDBj / Status: Released

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Structure visualization

Supplemental images

emd_31384.png

Downloads & links

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Map

FileDownload / File: emd_31384.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM single particle analysis of human Nup155 Longer N-terminus (19-1069)
Voxel sizeX=Y=Z: 0.823 Å
Density
Contour LevelBy AUTHOR: 0.26
Minimum - Maximum-1.2620121 - 2.5768025
Average (Standard dev.)-0.00012725238 (±0.04402893)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 230.44 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Purified human Nup155 protein

EntireName: Purified human Nup155 protein
Components
  • Organelle or cellular component: Purified human Nup155 protein
    • Protein or peptide: G protein/GFP fusion protein,Nuclear pore complex protein Nup155

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Supramolecule #1: Purified human Nup155 protein

SupramoleculeName: Purified human Nup155 protein / type: organelle_or_cellular_component / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Recombinant vesicular stomatitis Indiana virus rVSV-G/GFP
Molecular weightExperimental: 182 kDa/nm
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: G protein/GFP fusion protein,Nuclear pore complex protein Nup155

MacromoleculeName: G protein/GFP fusion protein,Nuclear pore complex protein Nup155
type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human) / Tissue: Kidney / Cell: Epithelial
Molecular weightTheoretical: 183.532594 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI DFKEDGNILG HKLEYNYNSH NVYIMADKQK N GIKVNFKI ...String:
MVSKGEELFT GVVPILVELD GDVNGHKFSV SGEGEGDATY GKLTLKFICT TGKLPVPWPT LVTTLTYGVQ CFSRYPDHMK QHDFFKSAM PEGYVQERTI FFKDDGNYKT RAEVKFEGDT LVNRIELKGI DFKEDGNILG HKLEYNYNSH NVYIMADKQK N GIKVNFKI RHNIEDGSVQ LADHYQQNTP IGDGPVLLPD NHYLSTQSAL SKDPNEKRDH MVLLEFVTAA GITLGMDELY KS GLRSRAQ ASNSMPSSLL GAAMPASTSA AALQEALENA GRLIDRQLQE DRMYPDLSEL LMVSAPNNPT VSGMSDMDYP LQG PGLLSV PNLPEISSIR RVPLPPELVE QFGHMQCNCM MGVFPPISRA WLTIDSDIFM WNYEDGGDLA YFDGLSETIL AVGL VKPKA GIFQPHVRHL LVLATPVDIV ILGLSYANLQ TGSGVLNDSL SGGMQLLPDP LYSLPTDNTY LLTITSTDNG RIFLA GKDG CLYEVAYQAE AGWFSQRCRK INHSKSSLSF LVPSLLQFTF SEDDPILQIA IDNSRNILYT RSEKGVIQVY DLGQDG QGM SRVASVSQNA IVSAAGNIAR TIDRSVFKPI VQIAVIENSE SLDCQLLAVT HAGVRLYFST CPFRQPLARP NTLTLVH VR LPPGFSASST VEKPSKVHRA LYSKGILLMA ASENEDNDIL WCVNHDTFPF QKPMMETQMT AGVDGHSWAL SAIDELKV D KIITPLNKDH IPITDSPVVV QQHMLPPKKF VLLSAQGSLM FHKLRPVDQL RHLLVSNVGG DGEEIERFFK LHQEDQACA TCLILACSTA ACDREVSAWA TRAFFRYGGE AQMRFPTTLP PPSNVGPILG SPVYSSSPVP SGSPYPNPSF LGTPSHGIQP PAMSTPVCA LGNPATQATN MSCVTGPEIV YSGKHNGICI YFSRIMGNIW DASLVVERIF KSGNREITAI ESSVPCQLLE S VLQELKGL QEFLDRNSQF AGGPLGNPNT TAKVQQRLIG FMRPENGNPQ QMQQELQRKF HEAQLSEKIS LQAIQQLVRK SY QALALWK LLCEHQFTII VAELQKELQE QLKITTFKDL VIRDKELTGA LIASLINCYI RDNAAVDGIS LHLQDICPLL YST DDAICS KANELLQRSR QVQNKTEKER MLRESLKEYQ KISNQVDLSN VCAQYRQVRF YEGVVELSLT AAEKKDPQGL GLHF YKHGE PEEDIVGLQA FQERLNSYKC ITDTLQELVN QSKAAPQSPS VPKKPGPPVL SSDPNMLSNE EAGHHFEQML KLSQR SKDE LFSIALYNWL IQVDLADKLL QVASPFLEPH LVRMAKVDQN RVRYMDLLWR YYEKNRSFSN AARVLSRLAD MHSTEI SLQ QRLEYIARAI LSAKSSTAIS SIAADGEFLH ELEEKMEVAR IQLQIQETLQ RQYSHHSSVQ DAVSQLDSEL MDITKLY GE FADPFKLAEC KLAIIHCAGY SDPILVQTLW QDIIEKELSD SVTLSSSDRM HALSLKIVLL GKIYAGTPRF FPLDFIVQ F LEQQVCTLNW DVGFVIQTMN EIGVPLPRLL EVYDQLFKSR DPFWNRMKKP LHLLDCIHVL LIRYVENPSQ VLNCERRRF TNLCLDAVCG YLVELQSMSS SVAVQAITGN FKSLQAKLER LH

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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

Concentration0.5 mg/mL
BufferpH: 7.5
Component:
ConcentrationFormulaName
50.0 mMTris-ClTris
150.0 mMNaClSodium chlorideSodium Chloride
0.05 mMDDMn-Dodecyl-B-D-Maltoside
1.0 mMEDTAEthylenediaminetetraacetic acidEthylenediamine tetraacetic acid
1.0 %GlycerolGlycerol

Details: Buffer was freshly made.
GridModel: Quantifoil R2/1 / Material: GOLD / Mesh: 200 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 291 K / Instrument: FEI VITROBOT MARK IV / Details: Blot for 3 seconds before plunging.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageCooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: COUNTING / Digitization - Frames/image: 3-46 / Average electron dose: 1.15 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 500000
CTF correctionSoftware - Name: RELION (ver. 3.1-beta)
Startup modelType of model: OTHER / Details: Nup155 Longer N-terminus structure (19-1069aa)
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: cryoSPARC (ver. v3.2.0)
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: cryoSPARC (ver. v3.2.0)
Final reconstructionResolution.type: BY AUTHOR / Resolution: 5.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. v3.2.0) / Number images used: 37100

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7eyq:
Cryo-EM (SPA) structure of human Nup155 Longer N-terminus (19-1069) at 5.4 Angstrom resolution

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