[English] 日本語
Yorodumi
- PDB-6p6a: Structure of Mouse Importin alpha - NIT2 NLS peptide complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6p6a
TitleStructure of Mouse Importin alpha - NIT2 NLS peptide complex
Components
  • Importin subunit alpha-1
  • Nitrogen catabolic enzyme regulatory protein
KeywordsTRANSPORT PROTEIN / nuclear import / importin alpha / transcription factor
Function / homology
Function and homology information


Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nitrate assimilation / cytoplasmic stress granule ...Sensing of DNA Double Strand Breaks / entry of viral genome into host nucleus through nuclear pore complex via importin / positive regulation of viral life cycle / NLS-dependent protein nuclear import complex / postsynapse to nucleus signaling pathway / nuclear import signal receptor activity / nuclear localization sequence binding / NLS-bearing protein import into nucleus / nitrate assimilation / cytoplasmic stress granule / protein import into nucleus / host cell / DNA-binding transcription factor binding / postsynaptic density / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / glutamatergic synapse / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / zinc ion binding / nucleoplasm / nucleus / cytosol
Similarity search - Function
Nitrogen regulatory protein areA, GATA-like domain / Fungal protein of unknown function (DUF1752) / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type / Importin subunit alpha / Atypical Arm repeat ...Nitrogen regulatory protein areA, GATA-like domain / Fungal protein of unknown function (DUF1752) / Transcription factor GATA / GATA-type zinc finger domain. / GATA-type zinc finger domain profile. / zinc finger binding to DNA consensus sequence [AT]GATA[AG] / GATA zinc finger / Zinc finger, GATA-type / Importin subunit alpha / Atypical Arm repeat / Importin-alpha, importin-beta-binding domain superfamily / Importin beta binding domain / Atypical Arm repeat / Importin-alpha, importin-beta-binding domain / IBB domain profile. / Armadillo/plakoglobin ARM repeat profile. / Armadillo/beta-catenin-like repeat / Leucine-rich Repeat Variant / Armadillo/beta-catenin-like repeats / Armadillo / Leucine-rich Repeat Variant / Zinc finger, NHR/GATA-type / Armadillo-like helical / Alpha Horseshoe / Armadillo-type fold / Mainly Alpha
Similarity search - Domain/homology
Nitrogen catabolic enzyme regulatory protein / Importin subunit alpha-1
Similarity search - Component
Biological speciesMus musculus (house mouse)
Neurospora crassa (fungus)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.151 Å
AuthorsBernardes, N.E. / Fukuda, C.A. / Silva, T.D. / Oliveira, H.C. / Fontes, M.R.M.
Funding support Brazil, 1items
OrganizationGrant numberCountry
Sao Paulo Research Foundation (FAPESP)2013/24705-3 Brazil
CitationJournal: Sci Rep / Year: 2020
Title: Comparative study of the interactions between fungal transcription factor nuclear localization sequences with mammalian and fungal importin-alpha.
Authors: Bernardes, N.E. / Fukuda, C.A. / da Silva, T.D. / de Oliveira, H.C. / de Barros, A.C. / Dreyer, T.R. / Bertolini, M.C. / Fontes, M.R.M.
History
DepositionJun 3, 2019Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 29, 2020Provider: repository / Type: Initial release
Revision 1.1Feb 12, 2020Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 11, 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
B: Importin subunit alpha-1
A: Nitrogen catabolic enzyme regulatory protein
C: Nitrogen catabolic enzyme regulatory protein


Theoretical massNumber of molelcules
Total (without water)53,0403
Polymers53,0403
Non-polymers00
Water5,152286
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)78.678, 90.180, 99.181
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number19
Space group name H-MP212121

-
Components

#1: Protein Importin subunit alpha-1 / Importin alpha P1 / Karyopherin subunit alpha-2 / Pendulin / Pore targeting complex 58 kDa subunit ...Importin alpha P1 / Karyopherin subunit alpha-2 / Pendulin / Pore targeting complex 58 kDa subunit / PTAC58 / RAG cohort protein 1 / SRP1-alpha


Mass: 49886.633 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Kpna2, Rch1
Production host: Escherichia coli 'BL21-Gold(DE3)pLysS AG' (bacteria)
References: UniProt: P52293
#2: Protein/peptide Nitrogen catabolic enzyme regulatory protein / Nitrogen regulatory protein 2 / NIT2


Mass: 1576.805 Da / Num. of mol.: 2 / Source method: obtained synthetically
Source: (synth.) Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) (fungus)
References: UniProt: P19212
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 286 / Source method: isolated from a natural source / Formula: H2O

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 3.32 Å3/Da / Density % sol: 66.51 %
Crystal growTemperature: 277 K / Method: vapor diffusion, hanging drop / pH: 6
Details: Sodium Citrate, DTT, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: LNLS / Beamline: W01B-MX2 / Wavelength: 1.425 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 16, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.425 Å / Relative weight: 1
ReflectionResolution: 2.151→36.57 Å / Num. obs: 38952 / % possible obs: 99.82 % / Redundancy: 12.7 % / Biso Wilson estimate: 33.73 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.1158 / Rpim(I) all: 0.03352 / Rrim(I) all: 0.1206 / Net I/σ(I): 2.28
Reflection shellResolution: 2.151→2.228 Å / Redundancy: 11.6 % / Rmerge(I) obs: 1.056 / Mean I/σ(I) obs: 0.819 / Num. unique obs: 3788 / CC1/2: 0.819 / Rpim(I) all: 0.3214 / % possible all: 99.11

-
Phasing

PhasingMethod: molecular replacement

-
Processing

Software
NameVersionClassification
PHENIX1.14_3260refinement
XDSdata scaling
PHENIXphasing
PDB_EXTRACT3.25data extraction
XDSdata reduction
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5U5P
Resolution: 2.151→36.568 Å / SU ML: 0.24 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 19.18
RfactorNum. reflection% reflection
Rfree0.1961 3705 5.02 %
Rwork0.1657 --
obs0.1672 73869 99.74 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 125.28 Å2 / Biso mean: 44.1196 Å2 / Biso min: 18.63 Å2
Refinement stepCycle: final / Resolution: 2.151→36.568 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3324 0 0 286 3610
Biso mean---49.55 -
Num. residues----437
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.151-2.17910.35481320.3132258995
2.1791-2.20890.29731430.27722695100
2.2089-2.24050.3081390.24672698100
2.2405-2.27390.25791430.23352707100
2.2739-2.30940.23121480.2192727100
2.3094-2.34730.24831440.21322690100
2.3473-2.38780.25511450.20592722100
2.3878-2.43120.21551430.19692691100
2.4312-2.47790.21191390.18842693100
2.4779-2.52850.23961430.18052711100
2.5285-2.58340.22121430.1852728100
2.5834-2.64350.20061420.17982663100
2.6435-2.70960.23011420.17152712100
2.7096-2.78290.18161420.15992702100
2.7829-2.86470.22241430.15892716100
2.8647-2.95710.20341360.1572678100
2.9571-3.06280.18251460.16712725100
3.0628-3.18530.22691410.16282705100
3.1853-3.33020.19271440.16352736100
3.3302-3.50570.18941450.16632677100
3.5057-3.72510.18461450.15332729100
3.7251-4.01240.16091370.13222689100
4.0124-4.41560.15331450.12752702100
4.4156-5.05310.16281470.13722713100
5.0531-6.36090.17631500.17422682100
6.3609-36.5680.17621380.1479268499
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL112)L122)L132)L222)L232)L332)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T112)T122)T132)T222)T232)T332)Origin x (Å)Origin y (Å)Origin z (Å)
11.2867-0.1927-0.46862.53121.08510.90880.10880.04640.1221-0.09230.00190.0146-0.1742-0.1145-0.11890.26370.00610.04080.23290.01690.186445.838992.827665.2624
20.95840.72741.04790.9090.79531.54970.09940.0858-0.21270.08230.0168-0.05690.08910.0385-0.1090.20640.0008-0.00180.2102-0.01050.27835.143162.32555.1989
30.9703-0.3328-0.12211.39490.30142.01530.10930.764-0.1897-0.64160.1126-0.39620.02320.488-0.13780.4660.0090.08660.7018-0.16770.444832.180251.049524.0072
43.0858-2.0137-0.47641.86151.2772.0757-0.27290.09670.3261-0.21630.24270.0499-0.14380.71390.0580.4376-0.08110.03670.5515-0.15020.547842.172957.408842.2602
56.00861.29662.3478.5882-1.93428.64280.3614-0.1266-0.4772-0.4547-0.3741.01730.2426-0.14360.00120.24090.0074-0.03050.3053-0.03450.249136.951486.216759.8142
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 72 through 202 )A72 - 202
2X-RAY DIFFRACTION2chain 'A' and (resid 203 through 390 )A203 - 390
3X-RAY DIFFRACTION3chain 'A' and (resid 391 through 497 )A391 - 497
4X-RAY DIFFRACTION4chain 'B' and (resid 129 through 133 )B129 - 133
5X-RAY DIFFRACTION5chain 'C' and (resid 127 through 132 )C127 - 132

+
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