[English] 日本語
Yorodumi
- PDB-7cyl: Crystal structure of Karyopherin-beta2 in complex with FUS PY-NLS... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 7cyl
TitleCrystal structure of Karyopherin-beta2 in complex with FUS PY-NLS(P525L)
Components
  • RNA-binding protein FUS
  • Transportin-1
KeywordsTRANSPORT PROTEIN/RNA BINDING PROTEIN / Nuclear import / Karyopherin / TRANSPORT PROTEIN / TRANSPORT PROTEIN-RNA BINDING PROTEIN complex
Function / homology
Function and homology information


Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / mRNA stabilization / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / intracellular non-membrane-bounded organelle / nuclear localization sequence binding / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination ...Tristetraprolin (TTP, ZFP36) binds and destabilizes mRNA / Intraflagellar transport / mRNA stabilization / Postmitotic nuclear pore complex (NPC) reformation / nuclear import signal receptor activity / intracellular non-membrane-bounded organelle / nuclear localization sequence binding / regulation of RNA splicing / Processing of Capped Intron-Containing Pre-mRNA / positive regulation of double-strand break repair via homologous recombination / mRNA Splicing - Major Pathway / RNA splicing / molecular condensate scaffold activity / mRNA 3'-UTR binding / transcription coregulator activity / protein homooligomerization / small GTPase binding / cilium / protein import into nucleus / amyloid fibril formation / transcription coactivator activity / chromatin binding / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / DNA binding / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus / metal ion binding / cytoplasm / cytosol
Similarity search - Function
TAF15/EWS/TLS family / Importin beta family / HEAT repeat / HEAT repeat / HEAT-like repeat / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Zinc finger domain ...TAF15/EWS/TLS family / Importin beta family / HEAT repeat / HEAT repeat / HEAT-like repeat / Importin-beta N-terminal domain profile. / Importin-beta N-terminal domain / Importin-beta N-terminal domain / Importin-beta, N-terminal domain / Zinc finger domain / Zn-finger in Ran binding protein and others / Zinc finger RanBP2 type profile. / Zinc finger RanBP2-type signature. / Zinc finger, RanBP2-type superfamily / Zinc finger, RanBP2-type / RNA recognition motif / RNA recognition motif / Eukaryotic RNA Recognition Motif (RRM) profile. / RNA recognition motif domain / RNA-binding domain superfamily / Armadillo-like helical / Armadillo-type fold / Nucleotide-binding alpha-beta plait domain superfamily
Similarity search - Domain/homology
RNA-binding protein FUS / Transportin-1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.7 Å
AuthorsYoshizawa, T. / Chook, Y.M.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM069909 United States
CitationJournal: Sci Rep / Year: 2021
Title: Mechanism of karyopherin-beta 2 binding and nuclear import of ALS variants FUS(P525L) and FUS(R495X).
Authors: Gonzalez, A. / Mannen, T. / Cagatay, T. / Fujiwara, A. / Matsumura, H. / Niesman, A.B. / Brautigam, C.A. / Chook, Y.M. / Yoshizawa, T.
History
DepositionSep 3, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 24, 2021Provider: repository / Type: Initial release
Revision 1.1Nov 29, 2023Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Transportin-1
B: RNA-binding protein FUS


Theoretical massNumber of molelcules
Total (without water)104,1142
Polymers104,1142
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2510 Å2
ΔGint-5 kcal/mol
Surface area37670 Å2
MethodPISA
Unit cell
Length a, b, c (Å)129.190, 158.366, 68.712
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Space group name HallP22ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x+1/2,y+1/2,-z
#4: -x,-y,z

-
Components

#1: Protein Transportin-1 / Karyopherin beta-2 / Importin beta-2 / M9 region interaction protein / MIP


Mass: 98325.352 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TNPO1, KPNB2, MIP1, TRN / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: Q92973
#2: Protein RNA-binding protein FUS / 75 kDa DNA-pairing protein / Oncogene FUS / Oncogene TLS / POMp75 / Translocated in liposarcoma protein


Mass: 5788.235 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: FUS, TLS / Production host: Escherichia coli K-12 (bacteria) / Strain (production host): K-12 / References: UniProt: P35637

-
Experimental details

-
Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

-
Sample preparation

CrystalDensity Matthews: 3.61 Å3/Da / Density % sol: 65.91 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / Details: 1 M Succinic acid (pH7.0), 1%(w/v) PEG MME2000

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-ID / Wavelength: 0.97915 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 19, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97915 Å / Relative weight: 1
ReflectionResolution: 2.7→47.06 Å / Num. obs: 39428 / % possible obs: 99.69 % / Redundancy: 7 % / Biso Wilson estimate: 75.89 Å2 / CC1/2: 0.999 / Net I/σ(I): 19.3
Reflection shellResolution: 2.7→2.8 Å / Mean I/σ(I) obs: 2.2 / Num. unique obs: 3860 / CC1/2: 0.815

-
Processing

Software
NameVersionClassification
PHENIX1.17.1_3660refinement
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4FDD
Resolution: 2.7→47.06 Å / SU ML: 0.311 / Cross valid method: FREE R-VALUE / σ(F): 1.36 / Phase error: 27.0032
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2284 1972 5 %
Rwork0.1963 37455 -
obs0.198 39427 99.72 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 90.23 Å2
Refinement stepCycle: LAST / Resolution: 2.7→47.06 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6827 0 0 0 6827
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01046972
X-RAY DIFFRACTIONf_angle_d1.45689462
X-RAY DIFFRACTIONf_chiral_restr0.09441078
X-RAY DIFFRACTIONf_plane_restr0.00991221
X-RAY DIFFRACTIONf_dihedral_angle_d20.70462632
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.7-2.770.32851370.30082613X-RAY DIFFRACTION98.74
2.77-2.840.32761380.28622632X-RAY DIFFRACTION99.93
2.84-2.930.2911400.25982648X-RAY DIFFRACTION99.86
2.93-3.020.3391370.25712612X-RAY DIFFRACTION99.93
3.02-3.130.27261410.24212673X-RAY DIFFRACTION99.86
3.13-3.250.26741400.23342640X-RAY DIFFRACTION99.68
3.25-3.40.26211390.22982645X-RAY DIFFRACTION99.93
3.4-3.580.2811400.22552668X-RAY DIFFRACTION100
3.58-3.80.24761410.20682670X-RAY DIFFRACTION100
3.81-4.10.23321410.18752682X-RAY DIFFRACTION99.93
4.1-4.510.22361410.16972676X-RAY DIFFRACTION99.93
4.51-5.160.19081420.17472710X-RAY DIFFRACTION99.96
5.16-6.50.24411450.21162744X-RAY DIFFRACTION99.97
6.5-47.060.16991500.15652842X-RAY DIFFRACTION98.55
Refinement TLS params.Method: refined / Origin x: 29.534630176 Å / Origin y: 40.7075505528 Å / Origin z: 30.7826833689 Å
111213212223313233
T0.531012596858 Å20.0350728124082 Å2-0.00679642924534 Å2-0.488887516363 Å2-0.0536421787596 Å2--0.405193575401 Å2
L1.17460007189 °2-0.268717522089 °20.422280770994 °2-0.760109088605 °2-0.381124378559 °2--0.349416598187 °2
S0.182831697563 Å °-0.0654599696842 Å °-0.15175322095 Å °-0.0686380443344 Å °-0.104401070647 Å °0.11581761067 Å °0.0644805496489 Å °-0.0312707256654 Å °0.042556881633 Å °
Refinement TLS groupSelection details: all

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbjlvh1.pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more