[English] 日本語
Yorodumi
- PDB-6sja: Structure of HPV16 E6 oncoprotein in complex with IRF3 LxxLL motif -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 6sja
TitleStructure of HPV16 E6 oncoprotein in complex with IRF3 LxxLL motif
Components
  • Maltose/maltodextrin-binding periplasmic protein,Interferon regulatory factor 3
  • Protein E6
KeywordsVIRAL PROTEIN / HPV16 E6 protein / IRF3 mutant / LxxLL motif
Function / homology
Function and homology information


symbiont-mediated suppression of host transcription / IRF3 mediated activation of type 1 IFN / MDA-5 signaling pathway / macrophage apoptotic process / programmed necrotic cell death / symbiont-mediated perturbation of host apoptosis / TRIF-dependent toll-like receptor signaling pathway / signal transduction involved in regulation of gene expression / regulation of proteolysis / IRF3-mediated induction of type I IFN ...symbiont-mediated suppression of host transcription / IRF3 mediated activation of type 1 IFN / MDA-5 signaling pathway / macrophage apoptotic process / programmed necrotic cell death / symbiont-mediated perturbation of host apoptosis / TRIF-dependent toll-like receptor signaling pathway / signal transduction involved in regulation of gene expression / regulation of proteolysis / IRF3-mediated induction of type I IFN / LRR FLII-interacting protein 1 (LRRFIP1) activates type I IFN production / positive regulation of type I interferon-mediated signaling pathway / activation of GTPase activity / positive regulation of cytokine production involved in inflammatory response / cGAS/STING signaling pathway / mRNA transcription / TRAF6 mediated IRF7 activation / toll-like receptor 4 signaling pathway / DNA-binding transcription activator activity / cytoplasmic pattern recognition receptor signaling pathway / type I interferon-mediated signaling pathway / immune system process / cellular response to exogenous dsRNA / detection of maltose stimulus / maltose transport complex / maltose binding / carbohydrate transport / positive regulation of interferon-alpha production / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / positive regulation of type I interferon production / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / antiviral innate immune response / lipopolysaccharide-mediated signaling pathway / TICAM1-dependent activation of IRF3/IRF7 / positive regulation of interferon-beta production / Regulation of innate immune responses to cytosolic DNA / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / Activation of IRF3, IRF7 mediated by TBK1, IKKε (IKBKE) / promoter-specific chromatin binding / Negative regulators of DDX58/IFIH1 signaling / PDZ domain binding / DDX58/IFIH1-mediated induction of interferon-alpha/beta / cellular response to virus / Evasion by RSV of host interferon responses / DNA-binding transcription repressor activity, RNA polymerase II-specific / ISG15 antiviral mechanism / Interferon gamma signaling / sequence-specific double-stranded DNA binding / SARS-CoV-1 activates/modulates innate immune responses / Interferon alpha/beta signaling / TRAF3-dependent IRF activation pathway / outer membrane-bounded periplasmic space / regulation of inflammatory response / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity / DNA-binding transcription activator activity, RNA polymerase II-specific / symbiont-mediated perturbation of host ubiquitin-like protein modification / defense response to virus / regulation of apoptotic process / positive regulation of canonical NF-kappaB signal transduction / sequence-specific DNA binding / host cell cytoplasm / periplasmic space / DNA-binding transcription factor activity, RNA polymerase II-specific / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / DNA-binding transcription factor activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / protein domain specific binding / innate immune response / virus-mediated perturbation of host defense response / DNA-templated transcription / DNA damage response / host cell nucleus / chromatin / regulation of transcription by RNA polymerase II / apoptotic process / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / nucleoplasm / identical protein binding / membrane / nucleus / metal ion binding / cytosol / cytoplasm
Similarity search - Function
E6 early regulatory protein / CRO Repressor / Interferon regulatory factor-3 / Interferon-regulatory factor 3 / Interferon-regulatory factor 3 / Interferon regulatory factor, conserved site / IRF tryptophan pentad repeat DNA-binding domain signature. / Interferon regulatory factor transcription factor / interferon regulatory factor / Interferon regulatory factor DNA-binding domain ...E6 early regulatory protein / CRO Repressor / Interferon regulatory factor-3 / Interferon-regulatory factor 3 / Interferon-regulatory factor 3 / Interferon regulatory factor, conserved site / IRF tryptophan pentad repeat DNA-binding domain signature. / Interferon regulatory factor transcription factor / interferon regulatory factor / Interferon regulatory factor DNA-binding domain / IRF tryptophan pentad repeat DNA-binding domain profile. / E6 early regulatory protein / E6 superfamily / Early Protein (E6) / SMAD-like domain superfamily / SMAD/FHA domain superfamily / Maltose/Cyclodextrin ABC transporter, substrate-binding protein / Solute-binding family 1, conserved site / Bacterial extracellular solute-binding proteins, family 1 signature. / Bacterial extracellular solute-binding protein / Bacterial extracellular solute-binding protein / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / 2-Layer Sandwich / Alpha Beta
Similarity search - Domain/homology
Protein E6 / Maltose/maltodextrin-binding periplasmic protein / Interferon regulatory factor 3
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Homo sapiens (human)
Human papillomavirus type 16
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.5 Å
AuthorsSuarez, I.P. / Cousido-Siah, A. / Bonhoure, A. / Mitschler, A. / Podjarny, A. / Trave, G.
Funding support France, United States, 3items
OrganizationGrant numberCountry
French League Against Cancerequipe labellisee 2015 and fellowship AB France
National Institutes of Health/National Cancer Institute (NIH/NCI)R01CA134737 United States
Foundation for Medical Research (France)fellowship to IPS France
CitationJournal: To be published
Title: Deciphering de molecular and structural interaction between IRF3 and HPV16 E6
Authors: Poirson, J. / Suarez, I.P. / Cousido-Siah, A. / Forster, A. / Chebaro, Y. / Mitschler, A. / Straub, M. / Altschuh, D. / Podjarny, A. / Trave, G. / Masson, M.
History
DepositionAug 13, 2019Deposition site: PDBE / Processing site: PDBE
Revision 1.0Sep 4, 2019Provider: repository / Type: Initial release
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _chem_comp.name / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Nov 10, 2021Group: Database references / Derived calculations / Structure summary
Category: chem_comp / database_2 / struct_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag
Revision 3.0Jul 20, 2022Group: Advisory / Atomic model ...Advisory / Atomic model / Author supporting evidence / Data collection / Derived calculations / Other / Refinement description / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / cell / entity / pdbx_audit_support / pdbx_entity_instance_feature / pdbx_entry_details / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly / pdbx_struct_assembly_prop / pdbx_struct_conn_angle / pdbx_struct_sheet_hbond / pdbx_unobs_or_zero_occ_atoms / pdbx_validate_torsion / refine / refine_hist / refine_ls_shell / reflns / reflns_shell / software / struct_conn / symmetry
Item: _cell.volume / _entity.pdbx_mutation ..._cell.volume / _entity.pdbx_mutation / _entity.pdbx_number_of_molecules / _pdbx_audit_support.funding_organization / _pdbx_entry_details.has_ligand_of_interest / _pdbx_struct_assembly.details / _pdbx_struct_assembly.method_details / _pdbx_struct_conn_angle.value / _pdbx_struct_sheet_hbond.range_2_auth_comp_id / _pdbx_struct_sheet_hbond.range_2_auth_seq_id / _pdbx_struct_sheet_hbond.range_2_label_comp_id / _pdbx_struct_sheet_hbond.range_2_label_seq_id / _refine.B_iso_max / _refine.B_iso_mean / _refine.B_iso_min / _refine.ls_R_factor_R_free / _refine.ls_R_factor_R_work / _refine.ls_R_factor_obs / _refine.ls_d_res_high / _refine.ls_d_res_low / _refine.ls_number_reflns_R_free / _refine.ls_number_reflns_R_work / _refine.ls_number_reflns_obs / _refine.ls_percent_reflns_R_free / _refine.ls_percent_reflns_obs / _refine.overall_SU_ML / _refine.pdbx_ls_cross_valid_method / _refine.pdbx_ls_sigma_F / _refine.pdbx_overall_phase_error / _refine.pdbx_solvent_shrinkage_radii / _refine.pdbx_solvent_vdw_probe_radii / _refine.pdbx_starting_model / _refine.pdbx_stereochemistry_target_values / _refine.solvent_model_details / _refine_hist.cycle_id / _refine_hist.d_res_high / _refine_hist.d_res_low / _refine_hist.number_atoms_solvent / _refine_hist.number_atoms_total / _refine_hist.pdbx_B_iso_mean_ligand / _refine_hist.pdbx_B_iso_mean_solvent / _refine_hist.pdbx_number_atoms_protein / _refine_hist.pdbx_number_residues_total / _reflns.B_iso_Wilson_estimate / _reflns.d_resolution_high / _reflns.d_resolution_low / _reflns.pdbx_Rmerge_I_obs / _reflns.pdbx_Rrim_I_all / _reflns.pdbx_chi_squared / _reflns.pdbx_number_measured_all / _reflns.pdbx_redundancy / _software.version / _struct_conn.pdbx_dist_value / _symmetry.space_group_name_Hall
Description: Missing anisotropic B-factor / Provider: author / Type: Coordinate replacement
Revision 3.1Jan 24, 2024Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: Maltose/maltodextrin-binding periplasmic protein,Interferon regulatory factor 3
B: Protein E6
hetero molecules


Theoretical massNumber of molelcules
Total (without water)61,1325
Polymers60,1722
Non-polymers9603
Water8,665481
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: surface plasmon resonance
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)97.659, 132.870, 43.025
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
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 Maltose/maltodextrin-binding periplasmic protein,Interferon regulatory factor 3 / MMBP / Maltodextrin-binding protein / Maltose-binding protein / MBP / IRF-3


Mass: 41733.203 Da / Num. of mol.: 1 / Mutation: E360A,K363A,D364A,K84A,K240A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli), (gene. exp.) Homo sapiens (human)
Gene: malE, b4034, JW3994, IRF3 / Production host: Escherichia coli (E. coli) / References: UniProt: P0AEX9, UniProt: Q14653
#2: Protein Protein E6


Mass: 18439.256 Da / Num. of mol.: 1 / Mutation: F1047R,C1080S,C1097S,C1111S,C1140S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Human papillomavirus type 16 / Gene: E6 / Production host: Escherichia coli (E. coli) / References: UniProt: P03126
#3: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D- ...alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-maltopentaose


Type: oligosaccharide / Mass: 828.719 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,5,4/[a2122h-1a_1-5]/1-1-1-1-1/a4-b1_b4-c1_c4-d1_d4-e1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}}}}LINUCSPDB-CARE
#4: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 481 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.32 Å3/Da / Density % sol: 46.97 %
Crystal growTemperature: 298 K / Method: evaporation / pH: 6.8 / Details: PEG 1500 30%

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 Å
DetectorType: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Apr 27, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 1.5→45.832 Å / Num. obs: 170435 / % possible obs: 98.1 % / Redundancy: 6.999 % / Biso Wilson estimate: 27.053 Å2 / CC1/2: 0.999 / Rmerge(I) obs: 0.068 / Rrim(I) all: 0.074 / Χ2: 1.062 / Net I/σ(I): 15.95 / Num. measured all: 1192946
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
1.5-1.596.7041.151.6518066628150269480.6181.24795.7
1.59-1.77.2990.7042.8618759326350257010.8530.75797.5
1.7-1.837.2070.3914.9817373624600241050.9430.42198
1.83-2.016.9230.2088.8815374322599222070.9820.22598.3
2.01-2.256.570.1115.6313287920487202240.9940.1298.7
2.25-2.597.3830.07324.8913196518046178750.9970.07899.1
2.59-3.177.1640.04935.810838315243151290.9990.05399.3
3.17-4.486.3510.03349.347450711791117320.9990.03699.5
4.48-45.8327.5950.02661.5849474655065140.9990.02899.5

-
Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4GIZ

4giz


Resolution: 1.5→45.83 Å / SU ML: 0.15 / Cross valid method: THROUGHOUT / σ(F): 1.36 / Phase error: 18.78 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1905 8529 5.01 %
Rwork0.159 161863 -
obs0.1606 170392 98.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 96.38 Å2 / Biso mean: 29.1974 Å2 / Biso min: 11.48 Å2
Refinement stepCycle: final / Resolution: 1.5→45.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4075 0 58 486 4619
Biso mean--28.88 37.54 -
Num. residues----517
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.5-1.520.32392550.29564922517790
1.52-1.530.2672890.26195404569397
1.53-1.550.3082820.24815317559997
1.55-1.570.23292810.23285330561197
1.57-1.590.25382860.2195405569197
1.59-1.610.25292810.21285309559097
1.61-1.640.22532870.20865337562497
1.64-1.660.25142860.20095421570798
1.66-1.690.2292800.195333561398
1.69-1.720.19662880.17345411569998
1.72-1.740.19552820.17165342562498
1.74-1.780.20872820.16855434571698
1.78-1.810.21482810.15875355563698
1.81-1.850.22012820.15645399568198
1.85-1.890.18362890.14955425571498
1.89-1.930.19832850.1465376566198
1.93-1.980.18262920.15065432572498
1.98-2.030.19962850.14785431571699
2.03-2.090.18312800.14865401568199
2.09-2.160.16952840.14185474575899
2.16-2.240.17122900.14285425571599
2.24-2.330.17312860.13995446573299
2.33-2.430.17612890.14615443573299
2.43-2.560.19472900.14835436572699
2.56-2.720.21132850.15775454573999
2.72-2.930.19982880.15885466575499
2.93-3.230.19632850.16865479576499
3.23-3.70.2032860.15545480576699
3.7-4.650.14632860.137154935779100
4.66-45.830.16972870.161154835770100

+
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