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- EMDB-6231: The export receptor Crm1 forms a dimer to promote nuclear export ... -

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Basic information

Entry
Database: EMDB / ID: EMD-6231
TitleThe export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA
Map dataRandom conical tilt reconstruction from negative-stain electron micrographs of a human Crm1/RanGTP dimer bound to the HIV-1 Rev-RRE complex.
Sample
  • Sample: A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex
  • Protein or peptide: Crm1XPO1
  • Protein or peptide: Ran
  • Protein or peptide: Rev
  • RNA: Rev Response Element
KeywordsRNA Nuclear Export / HIV-host interactions / Human Crm1 / Human Ran / HIV-1 Rev / HIV-1 Rev Response Element
Function / homology
Function and homology information


structural constituent of nuclear pore => GO:0017056 / small GTPase binding => GO:0031267 / HuR (ELAVL1) binds and stabilizes mRNA / protein binding / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of centrosome duplication / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus ...structural constituent of nuclear pore => GO:0017056 / small GTPase binding => GO:0031267 / HuR (ELAVL1) binds and stabilizes mRNA / protein binding / annulate lamellae / regulation of proteasomal ubiquitin-dependent protein catabolic process / regulation of centrosome duplication / RNA nuclear export complex / nuclear export signal receptor activity / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus / manchette / Regulation of cholesterol biosynthesis by SREBP (SREBF) / importin-alpha family protein binding / host cell nucleolus / regulation of protein export from nucleus / protein localization to nucleolus / Rev-mediated nuclear export of HIV RNA / Nuclear import of Rev protein / NEP/NS2 Interacts with the Cellular Export Machinery / tRNA processing in the nucleus / GTP metabolic process / Postmitotic nuclear pore complex (NPC) reformation / nucleocytoplasmic transport / MicroRNA (miRNA) biogenesis / DNA metabolic process / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / dynein intermediate chain binding / Minus-strand DNA synthesis / Plus-strand DNA synthesis / ribosomal subunit export from nucleus / Uncoating of the HIV Virion / 2-LTR circle formation / Vpr-mediated nuclear import of PICs / Early Phase of HIV Life Cycle / spermatid development / mitotic sister chromatid segregation / Integration of provirus / ribosomal small subunit export from nucleus / APOBEC3G mediated resistance to HIV-1 infection / protein localization to nucleus / ribosomal large subunit export from nucleus / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / mRNA transport / sperm flagellum / Binding and entry of HIV virion / Cajal body / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / mRNA export from nucleus / nuclear pore / Cyclin A/B1/B2 associated events during G2/M transition / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / viral life cycle / Resolution of Sister Chromatid Cohesion / NPAS4 regulates expression of target genes / protein export from nucleus / centriole / viral process / Downregulation of TGF-beta receptor signaling / mitotic spindle organization / G protein activity / male germ cell nucleus / RHO GTPases Activate Formins / Deactivation of the beta-catenin transactivating complex / hippocampus development / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / Transcriptional regulation by small RNAs / Assembly Of The HIV Virion / MAPK6/MAPK4 signaling / Heme signaling / Budding and maturation of HIV virion / kinetochore / recycling endosome / small GTPase binding / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / Separation of Sister Chromatids / melanosome / ribosome biogenesis / mitotic cell cycle / nuclear envelope / positive regulation of protein binding / midbody / actin cytoskeleton organization / nuclear membrane / host cell cytoplasm / cadherin binding / ribonucleoprotein complex / DNA-binding transcription factor activity / protein heterodimerization activity / cell division / protein domain specific binding / intracellular membrane-bounded organelle / GTPase activity / host cell nucleus / chromatin binding
Similarity search - Function
Anti-repression trans-activator protein, REV protein / Anti-repression trans-activator protein, REV protein / REV protein (anti-repression trans-activator protein) / Exportin-1, C-terminal / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat ...Anti-repression trans-activator protein, REV protein / Anti-repression trans-activator protein, REV protein / REV protein (anti-repression trans-activator protein) / Exportin-1, C-terminal / Exportin-1, C-terminal / Exportin-1, repeat 3 / Chromosome region maintenance repeat / Exportin-1, repeat 2 / CRM1 C terminal / Chromosome region maintenance or exportin repeat / CRM1 / Exportin repeat 2 / CRM1 / Exportin repeat 3 / CRM1 C terminal / Exportin-1/5 / Exportin-1/Importin-beta-like / Exportin-1/Importin-beta-like / Exportin 1-like protein / small GTPase Ran family profile. / Ran GTPase / Ran GTPase / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Importin-beta, N-terminal domain / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Small GTPase / Ras family / Rab subfamily of small GTPases / Armadillo-like helical / Armadillo-like helical / Small GTP-binding protein domain / Small GTP-binding protein domain / Armadillo-type fold / Armadillo-type fold / P-loop containing nucleoside triphosphate hydrolase / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Exportin-1 / Protein Rev / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesHomo sapiens (human) / Human immunodeficiency virus 1
Methodsingle particle reconstruction / negative staining / Resolution: 25.0 Å
AuthorsBooth DS / Cheng Y / Frankel AD
CitationJournal: Elife / Year: 2014
Title: The export receptor Crm1 forms a dimer to promote nuclear export of HIV RNA.
Authors: David S Booth / Yifan Cheng / Alan D Frankel /
Abstract: The HIV Rev protein routes viral RNAs containing the Rev Response Element (RRE) through the Crm1 nuclear export pathway to the cytoplasm where viral proteins are expressed and genomic RNA is ...The HIV Rev protein routes viral RNAs containing the Rev Response Element (RRE) through the Crm1 nuclear export pathway to the cytoplasm where viral proteins are expressed and genomic RNA is delivered to assembling virions. The RRE assembles a Rev oligomer that displays nuclear export sequences (NESs) for recognition by the Crm1-Ran(GTP) nuclear receptor complex. Here we provide the first view of an assembled HIV-host nuclear export complex using single-particle electron microscopy. Unexpectedly, Crm1 forms a dimer with an extensive interface that enhances association with Rev-RRE and poises NES binding sites to interact with a Rev oligomer. The interface between Crm1 monomers explains differences between Crm1 orthologs that alter nuclear export and determine cellular tropism for viral replication. The arrangement of the export complex identifies a novel binding surface to possibly target an HIV inhibitor and may point to a broader role for Crm1 dimerization in regulating host gene expression.
History
DepositionJan 4, 2015-
Header (metadata) releaseJan 14, 2015-
Map releaseJan 14, 2015-
UpdateFeb 10, 2016-
Current statusFeb 10, 2016Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.31
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.31
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

400_6231.gif

Downloads & links

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Map

FileDownload / File: emd_6231.map.gz / Format: CCP4 / Size: 1.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRandom conical tilt reconstruction from negative-stain electron micrographs of a human Crm1/RanGTP dimer bound to the HIV-1 Rev-RRE complex.
Voxel sizeX=Y=Z: 4.04 Å
Density
Contour LevelBy AUTHOR: 0.31 / Movie #1: 0.31
Minimum - Maximum-0.20516232 - 1.0428586
Average (Standard dev.)-0.0182145 (±0.09284244)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-40-40-40
Dimensions808080
Spacing808080
CellA=B=C: 323.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z4.044.044.04
M x/y/z808080
origin x/y/z0.0000.0000.000
length x/y/z323.200323.200323.200
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS-40-40-40
NC/NR/NS808080
D min/max/mean-0.2051.043-0.018

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Supplemental data

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Sample components

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Entire : A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex

EntireName: A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex
Components
  • Sample: A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex
  • Protein or peptide: Crm1XPO1
  • Protein or peptide: Ran
  • Protein or peptide: Rev
  • RNA: Rev Response Element

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Supramolecule #1000: A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex

SupramoleculeName: A dimer of human Crm1/RanGTP bound to the HIV Rev-RRE complex
type: sample / ID: 1000
Oligomeric state: Crm1/RanGTP dimer, HIV-1 Rev homohexamer, HIV-1 RRE monomer
Number unique components: 4
Molecular weightExperimental: 462 KDa / Theoretical: 457 KDa / Method: Multi-angle laser light scattering

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Macromolecule #1: Crm1

MacromoleculeName: Crm1 / type: protein_or_peptide / ID: 1 / Name.synonym: Xpo1 / Number of copies: 2 / Oligomeric state: Dimer / Recombinant expression: Yes
Source (natural)Organism: Homo sapiens (human) / synonym: Human / Organelle: Nucleus, cytoplasm
Molecular weightExperimental: 125 KDa / Theoretical: 124 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli) / Recombinant strain: BL21(DE3) / Recombinant plasmid: pET19b
SequenceUniProtKB: Exportin-1
GO: structural constituent of nuclear pore => GO:0017056, viral process, viral life cycle, small GTPase binding => GO:0031267
InterPro: Armadillo-type fold, Armadillo-like helical, Importin-beta, N-terminal domain, Exportin-1/Importin-beta-like, Exportin-1, C-terminal

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Macromolecule #2: Ran

MacromoleculeName: Ran / type: protein_or_peptide / ID: 2
Details: Mutation of Gln69Leu with guanosine tri-phosphate bound.
Number of copies: 2 / Oligomeric state: Monomer / Recombinant expression: Yes
Source (natural)Organism: Homo sapiens (human) / synonym: Human / Organelle: Nucleus, cytoplasm
Molecular weightExperimental: 26 KDa / Theoretical: 25 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli) / Recombinant strain: BL21(DE3) / Recombinant plasmid: pET19b
SequenceUniProtKB: GTP-binding nuclear protein Ran
GO: GTP binding, structural constituent of nuclear pore => GO:0017056, viral process, viral life cycle
InterPro: P-loop containing nucleoside triphosphate hydrolase, Ran GTPase, Small GTP-binding protein domain, Small GTPase

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Macromolecule #3: Rev

MacromoleculeName: Rev / type: protein_or_peptide / ID: 3 / Number of copies: 6 / Oligomeric state: Hexamer / Recombinant expression: Yes
Source (natural)Organism: Human immunodeficiency virus 1 / Strain: HXB3 / synonym: HIV-1 / Organelle: Nucleus, cytoplasm of host human cells
Molecular weightTheoretical: 13 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli) / Recombinant strain: BL21(DE3) / Recombinant plasmid: pHGB1
SequenceUniProtKB: Protein Rev
GO: viral process, viral life cycle, mRNA transport, RNA binding, host cell nucleus, host cell cytoplasm, protein binding
InterPro: Anti-repression trans-activator protein, REV protein

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Macromolecule #4: Rev Response Element

MacromoleculeName: Rev Response Element / type: rna / ID: 4 / Name.synonym: RRE
Details: 245-nucleotide portion of the 351-nucleotide Rev Response Element from the HIV-1 genome
Classification: OTHER / Structure: SINGLE STRANDED / Synthetic?: Yes
Source (natural)Organism: Human immunodeficiency virus 1 / Strain: SF-2 / synonym: HIV-1
Molecular weightTheoretical: 80 KDa
SequenceString: GGGCUAGUAG GAGCUAUGUU CCUUGGGUUC UUGGGAGCAG CAGGAAGCAC UAUGGGCGCA GUGUCAUUGA CGCUGACGGU ACAGGCCAGA CAAUUAUUGU CUGGUAUAGU GCAACAGCAG AACAAUUUGC UGAGGGCUAU UGAGGCGCAA CAACAUCUGU UGCAACUCAC ...String:
GGGCUAGUAG GAGCUAUGUU CCUUGGGUUC UUGGGAGCAG CAGGAAGCAC UAUGGGCGCA GUGUCAUUGA CGCUGACGGU ACAGGCCAGA CAAUUAUUGU CUGGUAUAGU GCAACAGCAG AACAAUUUGC UGAGGGCUAU UGAGGCGCAA CAACAUCUGU UGCAACUCAC AGUCUGGGGC AUCAAGCAGC UCCAGGCAAG AGUCCUGGCU GUGGAAAGAU ACCUAAGGGA UCAACAGCUC CUAGGGG

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Experimental details

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Structure determination

Methodnegative staining
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.1 mg/mL
BufferpH: 7.4
Details: 50 mM HEPES-KOH, 50 mM potassium chloride, 2 mM magnesium acetate, 2 mM 2-mercaptoethanol, 2% v/v glycerol
StainingType: NEGATIVE / Details: 0.75% w/v uranyl formate
GridDetails: 200 mesh copper grid with thin carbon support, glow discharged
VitrificationCryogen name: NONE / Instrument: OTHER

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Electron microscopy

MicroscopeFEI TECNAI 12
Electron beamAcceleration voltage: 120 kV / Electron source: LAB6
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2 mm / Nominal defocus max: 6.0 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 52000
Sample stageSpecimen holder model: SIDE ENTRY, EUCENTRIC / Tilt angle max: 60
Alignment procedureLegacy - Electron beam tilt params: 0
DateDec 5, 2012
Image recordingCategory: CCD / Film or detector model: GATAN ULTRASCAN 4000 (4k x 4k) / Number real images: 44 / Average electron dose: 40 e/Å2
Tilt angle min0

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Image processing

CTF correctionDetails: Each particle
Final two d classificationNumber classes: 5
Final reconstructionAlgorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 25.0 Å / Resolution method: OTHER / Software - Name: FREALIGN, Spider / Number images used: 845
DetailsRandom conical tilt reconstructions were generated from samples tilted to 60 degrees using angular parameters from class averages of untilted particles. The structure was further refined by projection matching using both tilted and untilted particles.

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Atomic model buiding 1

Initial modelPDB ID:

3gb8


Chain - Chain ID: A
SoftwareName: Chimera
DetailsA human Crm1 dimer was extracted from the unit cell of the crystal structure.
RefinementSpace: REAL / Protocol: RIGID BODY FIT / Target criteria: Correlation

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