[English] 日本語
Yorodumi
- PDB-2phe: Model for VP16 binding to PC4 -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 2phe
TitleModel for VP16 binding to PC4
Components
  • Alpha trans-inducing protein
  • TRANSCRIPTIONAL COACTIVATOR PC4
KeywordsTRANSCRIPTION / PC4 / VP16 / cofactor / activator
Function / homology
Function and homology information


replication compartment / negative regulation of DNA metabolic process / negative regulation of DNA duplex unwinding / regulation of viral transcription / DNA-templated viral transcription / RNA polymerase II promoter clearance / viral tegument / biological process involved in interaction with host / host cell cytoplasmic vesicle / positive regulation of transcription initiation by RNA polymerase II ...replication compartment / negative regulation of DNA metabolic process / negative regulation of DNA duplex unwinding / regulation of viral transcription / DNA-templated viral transcription / RNA polymerase II promoter clearance / viral tegument / biological process involved in interaction with host / host cell cytoplasmic vesicle / positive regulation of transcription initiation by RNA polymerase II / core promoter sequence-specific DNA binding / molecular function activator activity / single-stranded DNA binding / protein-containing complex assembly / DNA-binding transcription factor binding / transcription regulator complex / host cell cytoplasm / structural constituent of virion / transcription coactivator activity / host cell perinuclear region of cytoplasm / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / host cell nucleus / nucleolus / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding / extracellular exosome / nucleoplasm / identical protein binding / nucleus
Similarity search - Function
Alpha trans-inducing protein (Alpha-TIF) / Herpes simplex virus, Tegument protein VP16, C-terminal / Alpha trans-inducing (Alpha-TIF) superfamily / Alpha trans-inducing protein (Alpha-TIF) / Herpes simplex virus virion protein 16 C terminal / Alpha trans-inducing protein (Alpha-TIF) / RNA polymerase II transcriptional coactivator Sub1/Tcp4-like / Transcriptional coactivator p15 (PC4), C-terminal / Transcriptional Coactivator p15 (PC4) / Transcriptional Coactivator Pc4; Chain A ...Alpha trans-inducing protein (Alpha-TIF) / Herpes simplex virus, Tegument protein VP16, C-terminal / Alpha trans-inducing (Alpha-TIF) superfamily / Alpha trans-inducing protein (Alpha-TIF) / Herpes simplex virus virion protein 16 C terminal / Alpha trans-inducing protein (Alpha-TIF) / RNA polymerase II transcriptional coactivator Sub1/Tcp4-like / Transcriptional coactivator p15 (PC4), C-terminal / Transcriptional Coactivator p15 (PC4) / Transcriptional Coactivator Pc4; Chain A / ssDNA-binding transcriptional regulator / Transcriptional Co-activator pc4; Chain A / Roll / Mainly Beta
Similarity search - Domain/homology
Tegument protein VP16 / Activated RNA polymerase II transcriptional coactivator p15
Similarity search - Component
Biological speciesHomo sapiens (human)
Herpes simplex virus
MethodSOLUTION NMR / The model was calculated using HADDOCK
AuthorsJonker, H.R.A. / Wechselberger, R.W. / Boelens, R. / Folkers, G.E. / Kaptein, R.
CitationJournal: Biochemistry / Year: 2005
Title: Structural Properties of the Promiscuous VP16 Activation Domain
Authors: Jonker, H.R.A. / Wechselberger, R.W. / Boelens, R. / Folkers, G.E. / Kaptein, R.
History
DepositionApr 11, 2007Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 24, 2007Provider: repository / Type: Initial release
Revision 1.1May 1, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Mar 16, 2022Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_nmr_spectrometer / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _pdbx_nmr_spectrometer.model / _struct_ref_seq_dif.details
Revision 1.4May 22, 2024Group: Data collection / Category: chem_comp_atom / chem_comp_bond

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: TRANSCRIPTIONAL COACTIVATOR PC4
B: TRANSCRIPTIONAL COACTIVATOR PC4
C: Alpha trans-inducing protein


Theoretical massNumber of molelcules
Total (without water)18,4743
Polymers18,4743
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)10 / 200Top-ranked ensemble, according to the average interaction energy and buried surface area
RepresentativeModel #1lowest energy

-
Components

#1: Protein TRANSCRIPTIONAL COACTIVATOR PC4 / SUB1 homolog / Positive cofactor 4 / P15 / p14


Mass: 7784.024 Da / Num. of mol.: 2 / Fragment: c-terminal core domain / Mutation: N61A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: SUB1, PC4, RPO2TC1 / Plasmid: pET11a / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: P53999
#2: Protein/peptide Alpha trans-inducing protein / Vmw65 / ICP25 / VP16 protein / Alpha- TIF


Mass: 2906.115 Da / Num. of mol.: 1 / Fragment: part of activation domain
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Herpes simplex virus (type 1 / strain 17)
Genus: Simplexvirus / Species: Human herpesvirus 1 / Strain: 17 / Gene: UL48 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P06492

-
Experimental details

-
Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
11115N-HSQCs
22213C-HN(CA)CB
13113C-HNCO
24215N-NOESY-HSQC

-
Sample preparation

Details
Solution-IDContentsSolvent system
10.2 mM VP16ad U-15N or U15N,13C, 0-0.5 mM PC4 or PC4ctd, 50 or 400 mM KCl, 50 mM phosphate buffer pH 5.6, 2 M D6-Glycine, H2OH2O
20.2 mM PC4 or PC4ctd U-15N, 0-0.5 mM VP16ad, 50 or 400 mM KCl, 50 mM phosphate buffer pH 5.6, 2 M D6-Glycine, H2OH2O
Sample conditions
Conditions-IDIonic strengthpHPressure (kPa)Temperature (K)
1100-450 mM 5.6 1 atm298 K
2100-450 mM 5.6 1 atm305 K

-
NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AVANCEBrukerAVANCE5001
Bruker AVANCEBrukerAVANCE6002
Bruker AVANCEBrukerAVANCE7503
Varian INOVAVarianINOVA5004
Varian INOVAVarianINOVA7505

-
Processing

NMR software
NameVersionDeveloperClassification
XwinNMR3.xBruker Biospincollection
VNMR1Varian Inc.collection
NMRPipe2.4Delaglio et al.processing
Sparky3.11Goddard et al.data analysis
CNS1.1Brunger et al.structure solution
HADDOCK1.2Dominguez et al.refinement
RefinementMethod: The model was calculated using HADDOCK / Software ordinal: 1
Details: The structure represents a docking model. The starting structure for PC4 was taken from the PDB entry 1PCF.
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: Top-ranked ensemble, according to the average interaction energy and buried surface area
Conformers calculated total number: 200 / Conformers submitted total number: 10

+
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