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- PDB-6e83: Solution structure of ZZZ3 ZZ domain in complex with histone H3 tail -

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Basic information

Entry
Database: PDB / ID: 6.0E+83
TitleSolution structure of ZZZ3 ZZ domain in complex with histone H3 tail
Components
  • Histone H3
  • ZZ-type zinc finger-containing protein 3
KeywordsGENE REGULATION / ZZZ3 / ZZ domain / histone / chromatin
Function / homology
Function and homology information


ATAC complex / regulation of tubulin deacetylation / regulation of cell division / Formation of WDR5-containing histone-modifying complexes / regulation of embryonic development / Chromatin modifying enzymes / epigenetic regulation of gene expression / methylated histone binding / telomere organization / histone reader activity ...ATAC complex / regulation of tubulin deacetylation / regulation of cell division / Formation of WDR5-containing histone-modifying complexes / regulation of embryonic development / Chromatin modifying enzymes / epigenetic regulation of gene expression / methylated histone binding / telomere organization / histone reader activity / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / Assembly of the ORC complex at the origin of replication / DNA methylation / Condensation of Prophase Chromosomes / HCMV Late Events / Chromatin modifications during the maternal to zygotic transition (MZT) / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / PRC2 methylates histones and DNA / Defective pyroptosis / HDACs deacetylate histones / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / lysine-acetylated histone binding / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / HDMs demethylate histones / mitotic spindle / PKMTs methylate histone lysines / RMTs methylate histone arginines / Meiotic recombination / Pre-NOTCH Transcription and Translation / nucleosome assembly / Activation of anterior HOX genes in hindbrain development during early embryogenesis / HCMV Early Events / Transcriptional regulation of granulopoiesis / structural constituent of chromatin / nucleosome / gene expression / RUNX1 regulates transcription of genes involved in differentiation of HSCs / chromatin organization / Factors involved in megakaryocyte development and platelet production / HATs acetylate histones / Senescence-Associated Secretory Phenotype (SASP) / Oxidative Stress Induced Senescence / Estrogen-dependent gene expression / regulation of cell cycle / cadherin binding / Amyloid fiber formation / protein heterodimerization activity / nucleolus / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / extracellular exosome / zinc ion binding / extracellular region / nucleoplasm / membrane / nucleus
Similarity search - Function
ZZ-type zinc finger-containing protein 3 / ZZZ3, zinc finger, ZZ-type / Myb-type HTH DNA-binding domain profile. / Myb domain / Zinc finger ZZ-type signature. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Myb-like DNA-binding domain ...ZZ-type zinc finger-containing protein 3 / ZZZ3, zinc finger, ZZ-type / Myb-type HTH DNA-binding domain profile. / Myb domain / Zinc finger ZZ-type signature. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Myb-like DNA-binding domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Histone H3 signature 1. / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Homeobox-like domain superfamily / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold
Similarity search - Domain/homology
Histone H3.1 / ZZ-type zinc finger-containing protein 3
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / simulated annealing
AuthorsZhang, Y. / Kutateladze, T.G.
CitationJournal: Nat Commun / Year: 2018
Title: The ZZ-type zinc finger of ZZZ3 modulates the ATAC complex-mediated histone acetylation and gene activation.
Authors: Mi, W. / Zhang, Y. / Lyu, J. / Wang, X. / Tong, Q. / Peng, D. / Xue, Y. / Tencer, A.H. / Wen, H. / Li, W. / Kutateladze, T.G. / Shi, X.
History
DepositionJul 27, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 19, 2018Provider: repository / Type: Initial release
Revision 1.1Oct 3, 2018Group: Data collection / 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_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
B: ZZ-type zinc finger-containing protein 3
A: Histone H3
hetero molecules


Theoretical massNumber of molelcules
Total (without water)8,7184
Polymers8,5882
Non-polymers1312
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100structures with the lowest energy
RepresentativeModel #1lowest energy

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Components

#1: Protein ZZ-type zinc finger-containing protein 3


Mass: 7279.126 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ZZZ3 / Production host: Escherichia coli (E. coli) / References: UniProt: Q8IYH5
#2: Protein/peptide Histone H3 /


Mass: 1308.488 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) Homo sapiens (human) / References: UniProt: P68431*PLUS
#3: Chemical ChemComp-ZN / ZINC ION


Mass: 65.409 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: Zn

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDSample stateSpectrometer-IDType
1102isotropic23D HNCA
1112isotropic23D CBCA(CO)NH
1122isotropic23D HBHA(CO)NH
1132isotropic23D (H)CCH-TOCSY
1142isotropic23D HN(CA)CB
111isotropic23D CBCA(CO)NH
161isotropic23D HBHA(CO)NH
181isotropic23D (H)CCH-TOCSY
191isotropic22D 1H-1H TOCSY
121isotropic13D 1H-13C NOESY aliphatic
171isotropic13D 1H-15N NOESY
131isotropic13D filtered 1H-13C NOESY aliphatic
141isotropic13D filtered 1H-15N NOESY

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Sample preparation

Details
TypeSolution-IDContentsLabelSolvent system
solution12 mM [U-13C; U-15N] ZZ domain of ZZZ3, 10 mM Histone H3, 100 mM sodium chloride, 20 mM TRIS, 7 % [U-99% 2H] D2O, 90% H2O/10% D2O13C/15N complex90% H2O/10% D2O
solution24 mM [U-13C; U-15N] ZZ domain of ZZZ3, 100 mM sodium chloride, 20 mM TRIS, 7 % [U-99% 2H] D2O, 90% H2O/10% D2O13C/15N apo90% H2O/10% D2O
Sample
Conc. (mg/ml)ComponentIsotopic labelingSolution-ID
2 mMZZ domain of ZZZ3[U-13C; U-15N]1
10 mMHistone H3natural abundance1
100 mMsodium chloridenatural abundance1
20 mMTRISnatural abundance1
7 %D2O[U-99% 2H]1
4 mMZZ domain of ZZZ3[U-13C; U-15N]2
100 mMsodium chloridenatural abundance2
20 mMTRISnatural abundance2
7 %D2O[U-99% 2H]2
Sample conditionsIonic strength: 0.1 M / Label: conditions_1 / pH: 7 / Pressure: 1 atm / Temperature: 298 K

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Varian INOVAVarianINOVA9001
Varian INOVAVarianINOVA6002

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Processing

NMR software
NameDeveloperClassification
VNMRVariancollection
NMRDrawDelaglio, Grzesiek, Vuister, Zhu, Pfeifer and Baxprocessing
AnalysisCCPNchemical shift assignment
X-PLOR NIHSchwieters, Kuszewski, Tjandra and Clorestructure calculation
AMBERD.A. Case, I.Y. Ben-Shalom, S.R. Brozell, D.S. Cerutti, T.E. Cheatham, III, V.W.D. Cruzeiro, T.A. Darden, R.E. Duke, D. Ghoreishi, M.K. Gilson, H. Gohlke, A.W. Goetz, D. Greene, R Harris, N. Homeyer, S. Izadi, A. Kovalenko, T. Kurtzman, T.S. Lee, S. LeGrand, P. Li, C. Lin, J. Liu, T. Luchko, R. Luo, D.J. Mermelstein, K.M. Merz, Y. Miao, G. Monard, C. Nguyen, H. Nguyen, I. Omelyan, A. Onufriev, F. Pan, R. Qi, D.R. Roe, A. Roitberg, C. Sagui, S. Schott-Verdugo, J. Shen, C.L. Simmerling, J. Smith, R. Salomon-Ferrer, J. Swails, R.C. Walker, J. Wang, H. Wei, R.M. Wolf, X. Wu, L. Xiao, D.M. York and P.A. Kollmanrefinement
RefinementMethod: simulated annealing / Software ordinal: 5
NMR representativeSelection criteria: lowest energy
NMR ensembleConformer selection criteria: structures with the lowest energy
Conformers calculated total number: 100 / Conformers submitted total number: 20

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