[English] 日本語
Yorodumi
- PDB-8c43: Ternary structure of 14-3-3sigma, strep-tagged PKA-responsive ERa... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8c43
TitleTernary structure of 14-3-3sigma, strep-tagged PKA-responsive ERa phosphopeptide, and Fusicoccin-A.
Components
  • 14-3-3 protein sigma
  • Estrogen Receptor alpha phosphopeptide
KeywordsPEPTIDE BINDING PROTEIN / 14-3-3 / hub-protein / ERa F-domain phosphopeptide
Function / homology
Function and homology information


regulation of epidermal cell division / protein kinase C inhibitor activity / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / regulation of cell-cell adhesion / cAMP/PKA signal transduction / Regulation of localization of FOXO transcription factors / keratinocyte proliferation / phosphoserine residue binding ...regulation of epidermal cell division / protein kinase C inhibitor activity / positive regulation of epidermal cell differentiation / keratinocyte development / keratinization / regulation of cell-cell adhesion / cAMP/PKA signal transduction / Regulation of localization of FOXO transcription factors / keratinocyte proliferation / phosphoserine residue binding / Activation of BAD and translocation to mitochondria / negative regulation of keratinocyte proliferation / establishment of skin barrier / negative regulation of protein localization to plasma membrane / Chk1/Chk2(Cds1) mediated inactivation of Cyclin B:Cdk1 complex / SARS-CoV-2 targets host intracellular signalling and regulatory pathways / negative regulation of protein kinase activity / negative regulation of stem cell proliferation / SARS-CoV-1 targets host intracellular signalling and regulatory pathways / RHO GTPases activate PKNs / positive regulation of protein localization / positive regulation of cell adhesion / protein sequestering activity / protein export from nucleus / negative regulation of innate immune response / TP53 Regulates Transcription of Genes Involved in G2 Cell Cycle Arrest / release of cytochrome c from mitochondria / positive regulation of protein export from nucleus / stem cell proliferation / TP53 Regulates Metabolic Genes / Translocation of SLC2A4 (GLUT4) to the plasma membrane / intrinsic apoptotic signaling pathway in response to DNA damage / intracellular protein localization / regulation of protein localization / positive regulation of cell growth / regulation of cell cycle / cadherin binding / protein kinase binding / negative regulation of transcription by RNA polymerase II / signal transduction / extracellular space / extracellular exosome / identical protein binding / nucleus / cytoplasm / cytosol
Similarity search - Function
14-3-3 protein sigma / 14-3-3 proteins signature 2. / 14-3-3 protein, conserved site / 14-3-3 proteins signature 1. / 14-3-3 protein / 14-3-3 homologues / 14-3-3 domain / 14-3-3 domain superfamily / 14-3-3 protein
Similarity search - Domain/homology
De-acetylated Fusicoccin / 14-3-3 protein sigma
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.4 Å
AuthorsSomsen, B.A. / Ottmann, C.
Funding support Netherlands, 1items
OrganizationGrant numberCountry
Netherlands Organisation for Scientific Research (NWO)711.017.014 Netherlands
CitationJournal: J.Biol.Chem. / Year: 2023
Title: Molecular basis and dual ligand regulation of tetrameric estrogen receptor alpha /14-3-3 zeta protein complex.
Authors: Somsen, B.A. / Sijbesma, E. / Leysen, S. / Honzejkova, K. / Visser, E.J. / Cossar, P.J. / Obsil, T. / Brunsveld, L. / Ottmann, C.
History
DepositionDec 30, 2022Deposition site: PDBE / Processing site: PDBE
Revision 1.0Dec 27, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 13, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature / Item: _pdbx_entry_details.has_protein_modification

-
Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

-
Assembly

Deposited unit
A: 14-3-3 protein sigma
B: Estrogen Receptor alpha phosphopeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)29,3356
Polymers28,6232
Non-polymers7124
Water4,486249
1
A: 14-3-3 protein sigma
B: Estrogen Receptor alpha phosphopeptide
hetero molecules

A: 14-3-3 protein sigma
B: Estrogen Receptor alpha phosphopeptide
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,67012
Polymers57,2464
Non-polymers1,4238
Water724
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation4_555x,-y,-z1
Buried area5260 Å2
ΔGint-39 kcal/mol
Surface area22390 Å2
MethodPISA
Unit cell
Length a, b, c (Å)81.788, 112.035, 62.339
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

-
Components

#1: Protein 14-3-3 protein sigma / Epithelial cell marker protein 1 / Stratifin


Mass: 26542.914 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: GAMGS at the beginning (-5 to -1) are part of the expression tag
Source: (gene. exp.) Homo sapiens (human) / Gene: SFN, HME1 / Production host: Escherichia coli (E. coli) / References: UniProt: P31947
#2: Protein/peptide Estrogen Receptor alpha phosphopeptide


Mass: 2080.199 Da / Num. of mol.: 1 / Mutation: F591R; P592R / Source method: obtained synthetically
Details: This peptide is based on ERa residues 588-595 however with a C-terminal strep tag (PWSHQFEK) and two point mutations (F591R; P592R),This peptide is based on ERa residues 588-595 however with ...Details: This peptide is based on ERa residues 588-595 however with a C-terminal strep tag (PWSHQFEK) and two point mutations (F591R; P592R),This peptide is based on ERa residues 588-595 however with a C-terminal strep tag (PWSHQFEK) and two point mutations (F591R; P592R),This peptide is based on ERa residues 588-595 however with a C-terminal strep tag (PWSHQFEK) and two point mutations (F591R; P592R),This peptide is based on ERa residues 588-595 however with a C-terminal strep tag (PWSHQFEK) and two point mutations (F591R; P592R)
Source: (synth.) Homo sapiens (human)
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-SIT / De-acetylated Fusicoccin / [(2~{S})-2-[(1~{E},3~{R},4~{S},8~{R},9~{R},10~{R},11~{S},14~{S})-14-(methoxymethyl)-3,10-dimethyl-8-[(2~{S},3~{R},4~{S},5~{S},6~{R})-6-(2-methylbut-3-en-2-yloxymethyl)-3,4,5-tris(oxidanyl)oxan-2-yl]oxy-4,9-bis(oxidanyl)-6-tricyclo[9.3.0.0^{3,7}]tetradeca-1,6-dienyl]propyl] ethanoate


Mass: 638.786 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C34H54O11 / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 249 / Source method: isolated from a natural source / Formula: H2O
Has ligand of interestY
Has protein modificationY

-
Experimental details

-
Experiment

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

-
Sample preparation

CrystalDensity Matthews: 2.59 Å3/Da / Density % sol: 52.6 %
Crystal growTemperature: 277 K / Method: vapor diffusion, sitting drop
Details: 0.095 M Hepes pH 7.1, 0.19 M CaCl2, 25% PEG400, 5% glycerol

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, DESY / Beamline: P11 / Wavelength: 1.0332 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Apr 6, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.0332 Å / Relative weight: 1
ReflectionResolution: 1.4→45.34 Å / Num. obs: 53914 / % possible obs: 95.5 % / Redundancy: 13.9 % / CC1/2: 1 / Net I/σ(I): 23.8
Reflection shellResolution: 1.4→1.42 Å / Mean I/σ(I) obs: 2.7 / Num. unique obs: 2447 / CC1/2: 0.78

-
Processing

Software
NameVersionClassification
PHENIX1.20.1-4487refinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
REFMAC5.8.0267refinement
PDB_EXTRACTdata extraction
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4JC3

4jc3


Resolution: 1.4→45.34 Å / SU ML: 0.14 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 19.85 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.1916 5127 4.94 %
Rwork0.1793 --
obs0.1799 53888 95.21 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 1.4→45.34 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms1873 0 48 249 2170
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0072085
X-RAY DIFFRACTIONf_angle_d1.032847
X-RAY DIFFRACTIONf_dihedral_angle_d9.143334
X-RAY DIFFRACTIONf_chiral_restr0.073320
X-RAY DIFFRACTIONf_plane_restr0.008373
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.4-1.420.31811540.30132996X-RAY DIFFRACTION86
1.42-1.430.26771320.26433170X-RAY DIFFRACTION91
1.43-1.450.26861640.23973167X-RAY DIFFRACTION91
1.45-1.470.2561850.21813163X-RAY DIFFRACTION93
1.47-1.490.2232010.20313203X-RAY DIFFRACTION92
1.49-1.510.20181380.19963216X-RAY DIFFRACTION93
1.51-1.530.22221710.19773238X-RAY DIFFRACTION94
1.53-1.550.22221360.18863331X-RAY DIFFRACTION95
1.55-1.580.21721830.18593256X-RAY DIFFRACTION95
1.58-1.60.18551930.18183325X-RAY DIFFRACTION96
1.6-1.630.20751400.17883028X-RAY DIFFRACTION89
1.63-1.660.23851480.17493249X-RAY DIFFRACTION93
1.66-1.690.19811850.17213340X-RAY DIFFRACTION96
1.69-1.730.18381660.17553325X-RAY DIFFRACTION96
1.73-1.760.19812130.18043282X-RAY DIFFRACTION97
1.76-1.80.23361450.18813371X-RAY DIFFRACTION97
1.81-1.850.23931620.18743357X-RAY DIFFRACTION97
1.85-1.90.19722170.18883347X-RAY DIFFRACTION97
1.9-1.960.18051630.17283380X-RAY DIFFRACTION98
1.96-2.020.16561880.18693354X-RAY DIFFRACTION98
2.02-2.090.20451650.16653385X-RAY DIFFRACTION98
2.09-2.180.20931610.17133394X-RAY DIFFRACTION98
2.18-2.270.1821620.17633099X-RAY DIFFRACTION90
2.27-2.390.19311650.17063442X-RAY DIFFRACTION98
2.39-2.540.18941600.17333375X-RAY DIFFRACTION98
2.54-2.740.16832120.18463396X-RAY DIFFRACTION99
2.74-3.020.17311760.18993430X-RAY DIFFRACTION99
3.02-3.450.19672090.17493417X-RAY DIFFRACTION99
3.45-4.350.17871920.15613175X-RAY DIFFRACTION93
4.35-45.340.17191410.1773487X-RAY DIFFRACTION100

+
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