[English] 日本語
Yorodumi
- PDB-6q84: Crystal structure of RanGTP-Pdr6-eIF5A export complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6q84
TitleCrystal structure of RanGTP-Pdr6-eIF5A export complex
Components
  • Eukaryotic translation initiation factor 5A-1
  • GTP-binding nuclear protein Ran
  • Importin beta-like protein KAP122
KeywordsPROTEIN TRANSPORT / Importin-Beta family / biportin / nuclear export / translation factor
Function / homology
Function and homology information


positive regulation of cytoplasmic translational elongation through polyproline stretches / Hypusine synthesis from eIF5A-lysine / CAT tailing / translational frameshifting / positive regulation of translational termination / positive regulation of translational elongation / RNA nuclear export complex / pre-miRNA export from nucleus / snRNA import into nucleus / cellular response to mineralocorticoid stimulus ...positive regulation of cytoplasmic translational elongation through polyproline stretches / Hypusine synthesis from eIF5A-lysine / CAT tailing / translational frameshifting / positive regulation of translational termination / positive regulation of translational elongation / RNA nuclear export complex / 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 / 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 / MicroRNA (miRNA) biogenesis / nuclear import signal receptor activity / DNA metabolic process / translational elongation / regulation of cell size / dynein intermediate chain binding / ribosomal subunit export from nucleus / spermatid development / mitotic sister chromatid segregation / ribosomal small subunit export from nucleus / positive regulation of translational initiation / ribosomal large subunit export from nucleus / sperm flagellum / translation elongation factor activity / rescue of stalled ribosome / nuclear pore / translation initiation factor activity / protein export from nucleus / centriole / viral process / mitotic spindle organization / G protein activity / male germ cell nucleus / hippocampus development / Transcriptional regulation by small RNAs / Hydrolases; Acting on acid anhydrides; Acting on GTP to facilitate cellular and subcellular movement / recycling endosome / positive regulation of protein import into nucleus / protein import into nucleus / GDP binding / melanosome / ribosome binding / mitotic cell cycle / nuclear envelope / positive regulation of protein binding / midbody / actin cytoskeleton organization / cadherin binding / protein heterodimerization activity / cell division / protein domain specific binding / GTPase activity / chromatin binding / chromatin / GTP binding / nucleolus / perinuclear region of cytoplasm / magnesium ion binding / protein-containing complex / mitochondrion / RNA binding / extracellular exosome / nucleoplasm / membrane / nucleus / cytosol / cytoplasm
Similarity search - Function
: / Translation initiation factor 5A-like, N-terminal / Translation elongation factor, IF5A, hypusine site / Eukaryotic initiation factor 5A hypusine signature. / Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold / Translation elongation factor IF5A-like / Translation elongation factor, IF5A C-terminal / Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold / small GTPase Ran family profile. / Ran GTPase ...: / Translation initiation factor 5A-like, N-terminal / Translation elongation factor, IF5A, hypusine site / Eukaryotic initiation factor 5A hypusine signature. / Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold / Translation elongation factor IF5A-like / Translation elongation factor, IF5A C-terminal / Eukaryotic elongation factor 5A hypusine, DNA-binding OB fold / small GTPase Ran family profile. / Ran GTPase / SH3 type barrels. - #30 / Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases / Nucleic acid-binding proteins / Rho (Ras homology) subfamily of Ras-like small GTPases / Ras subfamily of RAS small GTPases / Small GTPase / Ras family / Rab subfamily of small GTPases / SH3 type barrels. / Armadillo-like helical / OB fold (Dihydrolipoamide Acetyltransferase, E2P) / Small GTP-binding protein domain / Translation protein SH3-like domain superfamily / Ribosomal protein L2, domain 2 / Armadillo-type fold / P-loop containing nucleotide triphosphate hydrolases / Roll / Nucleic acid-binding, OB-fold / Beta Barrel / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
GUANOSINE-5'-TRIPHOSPHATE / Eukaryotic translation initiation factor 5A-1 / Importin beta-like protein KAP122 / GTP-binding nuclear protein Ran
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.7 Å
AuthorsAksu, M. / Trakhanov, S. / Vera-Rodriguez, A. / Gorlich, D.
CitationJournal: J.Cell Biol. / Year: 2019
Title: Structural basis for the nuclear import and export functions of the biportin Pdr6/Kap122.
Authors: Aksu, M. / Trakhanov, S. / Vera Rodriguez, A. / Gorlich, D.
History
DepositionDec 14, 2018Deposition site: PDBE / Processing site: PDBE
Revision 1.0May 1, 2019Provider: repository / Type: Initial release
Revision 1.1May 8, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Jun 12, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Importin beta-like protein KAP122
B: GTP-binding nuclear protein Ran
C: Eukaryotic translation initiation factor 5A-1
D: Importin beta-like protein KAP122
E: GTP-binding nuclear protein Ran
F: Eukaryotic translation initiation factor 5A-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)319,51910
Polymers318,4246
Non-polymers1,0954
Water0
1
A: Importin beta-like protein KAP122
B: GTP-binding nuclear protein Ran
C: Eukaryotic translation initiation factor 5A-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,7595
Polymers159,2123
Non-polymers5472
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
D: Importin beta-like protein KAP122
E: GTP-binding nuclear protein Ran
F: Eukaryotic translation initiation factor 5A-1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,7595
Polymers159,2123
Non-polymers5472
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)139.540, 139.540, 346.570
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number173
Space group name H-MP63
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 3 through 129 or resid 141 through 386 or resid 395 through 1076))
21(chain D and (resid 3 through 103 or (resid 104...
12chain B
22chain E
13(chain C and (resid 18 through 46 or resid 57...
23chain F

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 3 through 129 or resid 141 through 386 or resid 395 through 1076))A3 - 129
121(chain A and (resid 3 through 129 or resid 141 through 386 or resid 395 through 1076))A141 - 386
131(chain A and (resid 3 through 129 or resid 141 through 386 or resid 395 through 1076))A395 - 1076
211(chain D and (resid 3 through 103 or (resid 104...D3 - 103
221(chain D and (resid 3 through 103 or (resid 104...D104
231(chain D and (resid 3 through 103 or (resid 104...D3 - 1076
112chain BB8 - 178
212chain EE8 - 178
113(chain C and (resid 18 through 46 or resid 57...C18 - 46
123(chain C and (resid 18 through 46 or resid 57...C57 - 85
133(chain C and (resid 18 through 46 or resid 57...C86
143(chain C and (resid 18 through 46 or resid 57...C17 - 153
153(chain C and (resid 18 through 46 or resid 57...C17 - 153
163(chain C and (resid 18 through 46 or resid 57...C17 - 153
173(chain C and (resid 18 through 46 or resid 57...C17 - 153
213chain FF18 - 153

NCS ensembles :
ID
1
2
3

-
Components

#1: Protein Importin beta-like protein KAP122 / Karyopherin-122 / Pleiotropic drug resistance regulatory protein 6


Mass: 123492.633 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: KAP122, PDR6, YGL016W / Plasmid: pQE-80 / Production host: Escherichia coli (E. coli) / Strain (production host): Top10 F' / References: UniProt: P32767
#2: Protein GTP-binding nuclear protein Ran / Androgen receptor-associated protein 24 / GTPase Ran / Ras-like protein TC4 / Ras-related nuclear protein


Mass: 20192.484 Da / Num. of mol.: 2 / Mutation: Q69L
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: RAN, ARA24, OK/SW-cl.81 / Plasmid: pQE-80 / Production host: Escherichia coli (E. coli) / Strain (production host): Top10 F' / References: UniProt: P62826
#3: Protein Eukaryotic translation initiation factor 5A-1 / eIF-5A-1 / Hypusine-containing protein HP2 / eIF-4D


Mass: 15526.687 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c / Gene: HYP2, TIF51A, YEL034W, SYGP-ORF21 / Plasmid: pQE-80 / Production host: Escherichia coli (E. coli) / Strain (production host): NEB Express / References: UniProt: P23301
#4: Chemical ChemComp-GTP / GUANOSINE-5'-TRIPHOSPHATE / Guanosine triphosphate


Mass: 523.180 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C10H16N5O14P3 / Comment: GTP, energy-carrying molecule*YM
#5: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Mg

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.06 Å3/Da / Density % sol: 59.79 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 5.3 / Details: 100 mM Sodium acetate pH 5.3 and 30% PEG 300

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9779 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Feb 17, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9779 Å / Relative weight: 1
Reflection twinOperator: h,-h-k,-l / Fraction: 0.28
ReflectionResolution: 3.7→49.173 Å / Num. obs: 40583 / % possible obs: 99.83 % / Redundancy: 10.8 % / CC1/2: 1 / Rpim(I) all: 0.03048 / Rrim(I) all: 0.1006 / Rsym value: 0.09578 / Net I/σ(I): 17.74
Reflection shellResolution: 3.7→3.832 Å / Redundancy: 10 % / Mean I/σ(I) obs: 0.89 / Num. unique obs: 4014 / CC1/2: 0.527 / Rpim(I) all: 0.9533 / Rrim(I) all: 3.081 / Rsym value: 2.926 / % possible all: 99.65

-
Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
PDB_EXTRACT3.24data extraction
XDSdata reduction
XSCALEdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.7→49.173 Å / Cross valid method: THROUGHOUT / σ(F): 2.24 / Phase error: 40.93
RfactorNum. reflection% reflection
Rfree0.2471 2422 3.01 %
Rwork0.2065 --
obs0.2273 40554 99.77 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 338.38 Å2 / Biso mean: 198.6075 Å2 / Biso min: 103.23 Å2
Refinement stepCycle: final / Resolution: 3.7→49.173 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms21141 0 66 0 21207
Biso mean--180.09 --
Num. residues----2641
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A9779X-RAY DIFFRACTION4.836TORSIONAL
12D9779X-RAY DIFFRACTION4.836TORSIONAL
21B1734X-RAY DIFFRACTION4.836TORSIONAL
22E1734X-RAY DIFFRACTION4.836TORSIONAL
31C1221X-RAY DIFFRACTION4.836TORSIONAL
32F1221X-RAY DIFFRACTION4.836TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 17

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.7008-3.77630.33741460.33254628477496
3.7763-3.85840.33491400.3134469460997
3.8584-3.94810.38961400.33474582472297
3.9481-4.04680.33441420.32264614475697
4.0468-4.15610.35171410.32024608474997
4.1561-4.27830.38011420.31434539468197
4.2783-4.41630.32181410.29124587472897
4.4163-4.5740.281440.27964599474397
4.574-4.7570.27611440.26874598474297
4.757-4.97320.29291440.25494616476097
4.9732-5.23510.25371420.25044568471097
5.2351-5.56250.26811440.25164618476297
5.5625-5.99120.27871420.25374560470297
5.9912-6.59250.30391420.22664590473297
6.5925-7.54280.26921410.22694586472797
7.5428-9.48920.19341420.16424566470897
9.4892-45.81760.21491440.17184597474196

+
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://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