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- PDB-9qop: Binary complex of human Importin-9 with one homodimer of Akirin-2 -

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Basic information

Entry
Database: PDB / ID: 9qop
TitleBinary complex of human Importin-9 with one homodimer of Akirin-2
Components
  • Akirin-2
  • Importin-9
KeywordsPROTEIN TRANSPORT / 20S proteasome / 20S / proteasome / nuclear import / akirin / akirin2 / importin 9 / importin
Function / homology
Function and homology information


proteasome localization / regulation of muscle cell differentiation / positive regulation of B cell activation / histone chaperone activity / nuclear protein quality control by the ubiquitin-proteasome system / positive regulation of adaptive immune response / embryo development ending in birth or egg hatching / positive regulation of innate immune response / nuclear import signal receptor activity / transcription repressor complex ...proteasome localization / regulation of muscle cell differentiation / positive regulation of B cell activation / histone chaperone activity / nuclear protein quality control by the ubiquitin-proteasome system / positive regulation of adaptive immune response / embryo development ending in birth or egg hatching / positive regulation of innate immune response / nuclear import signal receptor activity / transcription repressor complex / transcription coregulator activity / cerebral cortex development / positive regulation of interleukin-6 production / small GTPase binding / protein import into nucleus / nuclear envelope / histone binding / response to lipopolysaccharide / protein-macromolecule adaptor activity / adaptive immune response / defense response to bacterium / innate immune response / chromatin / enzyme binding / positive regulation of transcription by RNA polymerase II / nucleoplasm / identical protein binding / nucleus / membrane / cytosol / cytoplasm
Similarity search - Function
: / Importin-9 central HEAT repeats / Akirin / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta N-terminal domain profile. / Importin-beta, N-terminal domain / Armadillo-like helical / Armadillo-type fold
Similarity search - Domain/homology
Akirin-2 / Importin-9
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsBrunner, H.L. / Grundmann, L. / David, H.
Funding supportEuropean Union, Austria, 2items
OrganizationGrant numberCountry
H2020 Marie Curie Actions of the European Commission847548European Union
Austrian Science Fund10.55776/F79 Austria
CitationJournal: To Be Published
Title: A multivalent adaptor mechanism drives the nuclear import of proteasomes
Authors: Brunner, H. / Kalis, R.W. / Grundmann, L. / Hodakova, Z. / Koskova, Z. / Grishkovskaya, I. / de Almeida, M. / Hinterndorfer, M. / Hoefflin, S. / Andersch, F. / Kotisch, H. / Dickmanns, A. / ...Authors: Brunner, H. / Kalis, R.W. / Grundmann, L. / Hodakova, Z. / Koskova, Z. / Grishkovskaya, I. / de Almeida, M. / Hinterndorfer, M. / Hoefflin, S. / Andersch, F. / Kotisch, H. / Dickmanns, A. / Cuylen-Haering, S. / Zuber, J. / Haselbach, D.
History
DepositionMar 26, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 28, 2026Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Jan 28, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: Akirin-2
A: Importin-9
C: Akirin-2


Theoretical massNumber of molelcules
Total (without water)161,1133
Polymers161,1133
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein Akirin-2


Mass: 22525.582 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: AKIRIN2, C6orf166 / Production host: Escherichia coli (E. coli) / Strain (production host): BL(21)DE / References: UniProt: Q53H80
#2: Protein Importin-9 / Imp9 / Ran-binding protein 9 / RanBP9


Mass: 116062.320 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IPO9, IMP9, KIAA1192, RANBP9, HSPC273 / Production host: Escherichia coli (E. coli) / References: UniProt: Q96P70
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Ternary complex of the human 20S proteasome in complex with two dimers of Akirin-2 and Importin-9
Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 200 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 40 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameCategory
2EPUimage acquisition
8PHENIXmodel refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 360044 / Symmetry type: POINT
RefinementHighest resolution: 3.7 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.0044325
ELECTRON MICROSCOPYf_angle_d0.4955394
ELECTRON MICROSCOPYf_dihedral_angle_d5.4521076
ELECTRON MICROSCOPYf_chiral_restr00
ELECTRON MICROSCOPYf_plane_restr0.0041076

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