[English] 日本語
Yorodumi
- PDB-8iiz: Crystal structure of MBP fused GAS41 YEATS domain in complex with... -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: PDB / ID: 8iiz
TitleCrystal structure of MBP fused GAS41 YEATS domain in complex with H3K27ac peptide
Components
  • Histone H3.1
  • Maltodextrin-binding protein,YEATS domain-containing protein 4
KeywordsNUCLEAR PROTEIN / YEATS domain / Transcription / Complex / Histone modification
Function / homology
Function and homology information


modification-dependent protein binding / Activation of the TFAP2 (AP-2) family of transcription factors / regulation of double-strand break repair / NuA4 histone acetyltransferase complex / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / positive regulation of double-strand break repair via homologous recombination / Chromatin modifying enzymes ...modification-dependent protein binding / Activation of the TFAP2 (AP-2) family of transcription factors / regulation of double-strand break repair / NuA4 histone acetyltransferase complex / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / positive regulation of double-strand break repair via homologous recombination / Chromatin modifying enzymes / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / telomere organization / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / SIRT1 negatively regulates rRNA expression / epigenetic regulation of gene expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / : / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / HDMs demethylate histones / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / structural constituent of cytoskeleton / Pre-NOTCH Transcription and Translation / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / nuclear matrix / Transcriptional regulation of granulopoiesis / HCMV Early Events / structural constituent of chromatin / nucleosome / nucleosome assembly / mitotic cell cycle / chromatin organization / HATs acetylate histones / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / outer membrane-bounded periplasmic space / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / regulation of apoptotic process / gene expression / nuclear membrane / Estrogen-dependent gene expression / histone binding / regulation of cell cycle / cadherin binding / chromatin remodeling / Amyloid fiber formation / protein heterodimerization activity / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / protein-containing complex / DNA binding / extracellular exosome / extracellular region / nucleoplasm / nucleus / membrane
Similarity search - Function
YEATS / : / YEATS superfamily / YEATS family / YEATS domain profile. / 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 ...YEATS / : / YEATS superfamily / YEATS family / YEATS domain profile. / 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 / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold
Similarity search - Domain/homology
alpha-maltose / Maltodextrin-binding protein / YEATS domain-containing protein 4 / Histone H3.1
Similarity search - Component
Biological speciesEscherichia coli (E. coli)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsKikuchi, M. / Umehara, T.
Funding support Japan, 1items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS) Japan
CitationJournal: Proc.Natl.Acad.Sci.USA / Year: 2023
Title: GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.
Authors: Kikuchi, M. / Takase, S. / Konuma, T. / Noritsugu, K. / Sekine, S. / Ikegami, T. / Ito, A. / Umehara, T.
History
DepositionFeb 24, 2023Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Nov 1, 2023Provider: repository / Type: Initial release
Revision 1.1Nov 15, 2023Group: Data collection / Category: chem_comp_atom / chem_comp_bond / Item: _chem_comp_atom.atom_id / _chem_comp_bond.atom_id_2
Revision 1.2Oct 23, 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: Maltodextrin-binding protein,YEATS domain-containing protein 4
B: Histone H3.1
C: Histone H3.1
hetero molecules


Theoretical massNumber of molelcules
Total (without water)64,6097
Polymers63,9913
Non-polymers6194
Water1,874104
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: isothermal titration calorimetry
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area3290 Å2
ΔGint-4 kcal/mol
Surface area22860 Å2
MethodPISA
Unit cell
Length a, b, c (Å)66.200, 66.200, 248.583
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number154
Space group name H-MP3221

-
Components

#1: Protein Maltodextrin-binding protein,YEATS domain-containing protein 4 / Glioma-amplified sequence 41 / Gas41 / NuMA-binding protein 1 / NuBI-1 / NuBI1


Mass: 57212.938 Da / Num. of mol.: 1 / Mutation: D108A, K109A, E198A, N199A, K265A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Escherichia coli (E. coli), (gene. exp.) Homo sapiens (human)
Gene: YEATS4, GAS41 / Production host: Escherichia coli (E. coli) / References: UniProt: C3SHQ8, UniProt: O95619
#2: Protein/peptide Histone H3.1 / Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone ...Histone H3/a / Histone H3/b / Histone H3/c / Histone H3/d / Histone H3/f / Histone H3/h / Histone H3/i / Histone H3/j / Histone H3/k / Histone H3/l


Mass: 3388.944 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431
#3: Polysaccharide alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: oligosaccharide / References: alpha-maltose
DescriptorTypeProgram
DGlcpa1-4DGlcpa1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(4+1)][a-D-Glcp]{}}LINUCSPDB-CARE
#4: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 104 / 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: 2.46 Å3/Da / Density % sol: 49.94 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop
Details: 100 mM Tris buffer (pH 8.5) containing 20% (w/v) PEG monomethyl ether 2000, 200 mM trimethylamine N-oxide

-
Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL26B2 / Wavelength: 1 Å
DetectorType: RAYONIX MX225-HS / Detector: CCD / Date: Apr 8, 2019
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.1→50 Å / Num. obs: 34835 / % possible obs: 91.1 % / Redundancy: 10.9 % / Rsym value: 0.118 / Net I/σ(I): 9.9
Reflection shellResolution: 2.1→2.17 Å / Mean I/σ(I) obs: 1.6 / Num. unique obs: 3093 / Rsym value: 1.502

-
Processing

Software
NameVersionClassification
REFMAC5.8.0267refinement
XDSdata reduction
Aimlessdata scaling
MOLREPphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.1→45.004 Å / Cor.coef. Fo:Fc: 0.937 / Cor.coef. Fo:Fc free: 0.907 / SU B: 8.117 / SU ML: 0.198 / Cross valid method: THROUGHOUT / ESU R: 0.288 / ESU R Free: 0.24
Details: Hydrogens have been added in their riding positions
RfactorNum. reflection% reflection
Rfree0.3009 1617 4.753 %
Rwork0.2496 32405 -
all0.252 --
obs-34022 89.308 %
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK BULK SOLVENT
Displacement parametersBiso mean: 48.36 Å2
Baniso -1Baniso -2Baniso -3
1--0.002 Å2-0.001 Å2-0 Å2
2---0.002 Å20 Å2
3---0.007 Å2
Refinement stepCycle: LAST / Resolution: 2.1→45.004 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms4055 0 41 104 4200
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0050.0134204
X-RAY DIFFRACTIONr_bond_other_d0.0010.0173940
X-RAY DIFFRACTIONr_angle_refined_deg1.3081.6545717
X-RAY DIFFRACTIONr_angle_other_deg1.1731.5879098
X-RAY DIFFRACTIONr_dihedral_angle_1_deg6.785523
X-RAY DIFFRACTIONr_dihedral_angle_2_deg31.63924.574188
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.31315664
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.81159
X-RAY DIFFRACTIONr_chiral_restr0.0530.2565
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.024738
X-RAY DIFFRACTIONr_gen_planes_other0.0010.02904
X-RAY DIFFRACTIONr_nbd_refined0.190.2898
X-RAY DIFFRACTIONr_symmetry_nbd_other0.1720.23782
X-RAY DIFFRACTIONr_nbtor_refined0.1630.22038
X-RAY DIFFRACTIONr_symmetry_nbtor_other0.0750.21869
X-RAY DIFFRACTIONr_xyhbond_nbd_refined0.1510.2159
X-RAY DIFFRACTIONr_symmetry_nbd_refined0.2020.211
X-RAY DIFFRACTIONr_nbd_other0.1510.250
X-RAY DIFFRACTIONr_symmetry_xyhbond_nbd_refined0.1360.210
X-RAY DIFFRACTIONr_mcbond_it2.7945.0992101
X-RAY DIFFRACTIONr_mcbond_other2.7945.0962100
X-RAY DIFFRACTIONr_mcangle_it4.3027.6372620
X-RAY DIFFRACTIONr_mcangle_other4.3017.642621
X-RAY DIFFRACTIONr_scbond_it2.7045.2722103
X-RAY DIFFRACTIONr_scbond_other2.7035.2732104
X-RAY DIFFRACTIONr_scangle_it4.3087.7883096
X-RAY DIFFRACTIONr_scangle_other4.3077.7893097
X-RAY DIFFRACTIONr_lrange_it6.32959.554696
X-RAY DIFFRACTIONr_lrange_other6.32859.5594697
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 20

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRfactor allNum. reflection allFsc freeFsc work% reflection obs (%)WRfactor Rwork
2.1-2.1540.6421300.65426440.65327910.6590.66499.39090.7
2.154-2.2130.569940.5718840.5726960.1650.22973.3680.606
2.213-2.2770.818100.8451910.84426010.0220.0247.72780.842
2.277-2.3470.3761060.322710.30325430.7440.82993.47230.274
2.347-2.4240.321910.28223700.28424610.8290.8391000.256
2.424-2.5090.3271080.26422830.26623910.8350.8761000.236
2.509-2.6030.3491280.24921870.25423150.840.8891000.223
2.603-2.7090.361140.26321140.26822280.8330.8751000.239
2.709-2.8290.332840.26520550.26821390.8240.8631000.244
2.829-2.9670.277970.22319610.22520580.8910.9141000.21
2.967-3.1260.3161070.23318660.23719730.8770.9131000.223
3.126-3.3150.274980.23417770.23618750.8940.9121000.231
3.315-3.5430.301700.22316550.22617250.8890.9211000.228
3.543-3.8240.24620.22511700.22616640.9150.9374.03850.229
3.824-4.1860.222550.19211350.19415220.9450.95278.18660.211
4.186-4.6750.249880.17813090.18213970.9370.9541000.206
4.675-5.3890.205590.16811750.1712340.960.9671000.194
5.389-6.5770.331510.20610290.21110800.9070.9391000.232
6.577-9.2030.22360.1878180.1898540.9330.9541000.222
9.203-45.0040.25290.2125110.2145400.9440.9661000.247

+
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